EzCatDB: D00471
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DB codeD00471
RLCP classification1.13.200.966 : Hydrolysis
CATH domainDomain 12.40.70.10 : Cathepsin D, subunit A; domain 1Catalytic domain
Domain 22.40.70.10 : Cathepsin D, subunit A; domain 1Catalytic domain
E.C.3.4.23.16,2.7.7.49,2.7.7.7,3.1.26.4
CSA1a30,1hiv
MACiEM0175

CATH domainRelated DB codes (homologues)
2.40.70.10 : Cathepsin D, subunit A; domain 1D00436,D00438,D00439,D00440,D00441,D00442,D00443,D00437,D00444,D00423,D00445,D00484,M00206,M00166,D00231,D00529

Enzyme Name
UniProtKBKEGG

P03366P04585P04587P35963
Protein nameGag-Pol polyproteinGag-Pol polyproteinGag-Pol polyproteinGag-Pol polyproteinHIV-1 retropepsin
human immunodeficiency virus type 1 protease
gag protease
HIV aspartyl protease
HIV proteinase
retroproteinase
HIV-1 protease
HIV-2 protease
SynonymsPr160Gag-Pol
Pr160Gag-Pol
Pr160Gag-Pol
Pr160Gag-Pol
ContainsMatrix protein p17
(MA)
Capsid protein p24
(CA)
Spacer peptide p2
Nucleocapsid protein p7
(NC)
Transframe peptide
(TF)
p6-pol
(p6*)
Protease
   EC 3.4.23.16
Retropepsin PR
Reverse transcriptase/ribonuclease H
   EC 2.7.7.49
   EC 2.7.7.7
   EC 3.1.26.4
p66 RT
p51 RT
p15
Integrase
(IN)
Matrix protein p17
(MA)
Capsid protein p24
(CA)
Spacer peptide p2
Nucleocapsid protein p7
(NC)
Transframe peptide
(TF)
p6-pol
(p6*)
Protease
   EC 3.4.23.16
Retropepsin PR
Reverse transcriptase/ribonuclease H
   EC 2.7.7.49
   EC 2.7.7.7
   EC 3.1.26.4
p66 RT
p51 RT
p15
Integrase
(IN)
Matrix protein p17
(MA)
Capsid protein p24
(CA)
Spacer peptide p2
Nucleocapsid protein p7
(NC)
Transframe peptide
(TF)
p6-pol
(p6*)
Protease
   EC 3.4.23.16
Retropepsin PR
Reverse transcriptase/ribonuclease H
   EC 2.7.7.49
   EC 2.7.7.7
   EC 3.1.26.4
p66 RT
p51 RT
p15
Integrase
(IN)
Matrix protein p17
(MA)
Capsid protein p24
(CA)
Spacer peptide p2
Nucleocapsid protein p7
(NC)
Transframe peptide
(TF)
p6-pol
(p6*)
Protease
   EC 3.4.23.16
Retropepsin PR
Reverse transcriptase/ribonuclease H
   EC 2.7.7.49
   EC 2.7.7.7
   EC 3.1.26.4
p66 RT
p51 RT
p15
Integrase
(IN)
RefSeq
NP_057849.4 (Protein)
NC_001802.1 (DNA/RNA sequence)


PfamPF00540 (Gag_p17)
PF00607 (Gag_p24)
PF00552 (IN_DBD_C)
PF02022 (Integrase_Zn)
PF00075 (RNase_H)
PF00665 (rve)
PF00077 (RVP)
PF00078 (RVT_1)
PF06815 (RVT_connect)
PF06817 (RVT_thumb)
PF00098 (zf-CCHC)
[Graphical view]
PF00540 (Gag_p17)
PF00607 (Gag_p24)
PF00552 (IN_DBD_C)
PF02022 (Integrase_Zn)
PF00075 (RNase_H)
PF00665 (rve)
PF00077 (RVP)
PF00078 (RVT_1)
PF06815 (RVT_connect)
PF06817 (RVT_thumb)
PF00098 (zf-CCHC)
[Graphical view]
PF00540 (Gag_p17)
PF00607 (Gag_p24)
PF00552 (IN_DBD_C)
PF02022 (Integrase_Zn)
PF00075 (RNase_H)
PF00665 (rve)
PF00077 (RVP)
PF00078 (RVT_1)
PF06815 (RVT_connect)
PF06817 (RVT_thumb)
PF00098 (zf-CCHC)
[Graphical view]
PF00540 (Gag_p17)
PF00607 (Gag_p24)
PF00552 (IN_DBD_C)
PF02022 (Integrase_Zn)
PF00075 (RNase_H)
PF00665 (rve)
PF00077 (RVP)
PF00078 (RVT_1)
PF06815 (RVT_connect)
PF06817 (RVT_thumb)
PF00098 (zf-CCHC)
[Graphical view]


UniProtKB:Accession NumberP03366P04585P04587P35963
Entry namePOL_HV1B1POL_HV1H2POL_HV1B5POL_HV1Y2
ActivitySpecific for a P1 residue that is hydrophobic, and P1'' variable, but often Pro.,Endonucleolytic cleavage to 5''- phosphomonoester.,Deoxynucleoside triphosphate + DNA(n) = diphosphate + DNA(n+1).Specific for a P1 residue that is hydrophobic, and P1'' variable, but often Pro.,Endonucleolytic cleavage to 5''- phosphomonoester.,Deoxynucleoside triphosphate + DNA(n) = diphosphate + DNA(n+1).Specific for a P1 residue that is hydrophobic, and P1'' variable, but often Pro.,Endonucleolytic cleavage to 5''- phosphomonoester.,Deoxynucleoside triphosphate + DNA(n) = diphosphate + DNA(n+1).Specific for a P1 residue that is hydrophobic, and P1'' variable, but often Pro.,Endonucleolytic cleavage to 5''- phosphomonoester.,Deoxynucleoside triphosphate + DNA(n) = diphosphate + DNA(n+1).
SubunitPre-integration complex interacts with human HMGA1. Matrix protein p17 is a trimer. Interacts with gp120 and human BAF. Capsid is a homodimer. Interacts with human PPIA/CYPA. The protease is a homodimer, whose active site consists of two apposed aspartic acid residues. The reverse transcriptase is a heterodimer of p66 RT and p51 RT (RT p66/p51). Heterodimerization of RT is essential for DNA polymerase activity. Despite the sequence identities, p66 RT and p51 RT have distinct folding. Integrase is a homodimer and possibly can form homotetramer. Integrase interacts with human SMARCB1/INI1 and human PSIP1/LEDGF isoform 1 (By similarity).Pre-integration complex interacts with human HMGA1. Matrix protein p17 is a trimer. Interacts with gp120 and human BAF. Capsid is a homodimer. Interacts with human PPIA/CYPA. The protease is a homodimer, whose active site consists of two apposed aspartic acid residues. The reverse transcriptase is a heterodimer of p66 RT and p51 RT (RT p66/p51). Heterodimerization of RT is essential for DNA polymerase activity. Despite the sequence identities, p66 RT and p51 RT have distinct folding. Integrase is a homodimer and possibly can form homotetramer. Integrase interacts with human SMARCB1/INI1 and human PSIP1/LEDGF isoform 1.Pre-integration complex interacts with human HMGA1. Matrix protein p17 is a trimer. Interacts with gp120 and human BAF. Capsid is a homodimer. Interacts with human PPIA/CYPA. The protease is a homodimer, whose active site consists of two apposed aspartic acid residues. The reverse transcriptase is a heterodimer of p66 RT and p51 RT (RT p66/p51). Heterodimerization of RT is essential for DNA polymerase activity. Despite the sequence identities, p66 RT and p51 RT have distinct folding. Integrase is a homodimer and possibly can form homotetramer. Integrase interacts with human SMARCB1/INI1 and human PSIP1/LEDGF isoform 1 (By similarity).Pre-integration complex interacts with human HMGA1. Matrix protein p17 is a trimer. Interacts with gp120 and human BAF. Capsid is a homodimer. Interacts with human PPIA/CYPA. The protease is a homodimer, whose active site consists of two apposed aspartic acid residues. The reverse transcriptase is a heterodimer of p66 RT and p51 RT (RT p66/p51). Heterodimerization of RT is essential for DNA polymerase activity. Despite the sequence identities, p66 RT and p51 RT have distinct folding. Integrase is a homodimer and possibly can form homotetramer. Integrase interacts with human SMARCB1/INI1 and human PSIP1/LEDGF isoform 1 (By similarity).
Subcellular locationMatrix protein p17: Virion (Potential). Nucleus (By similarity). Cytoplasm (By similarity). Cell membrane, Lipid-anchor (Potential). Note=Following virus entry, the nuclear localization signal (NLS) of the matrix protein participates with Vpr to the nuclear localization of the viral genome. During virus production, the nuclear export activity of the matrix protein counteracts the NLS to maintain the Gag and Gag-Pol polyproteins in the cytoplasm, thereby directing unspliced RNA to the plasma membrane (By similarity).,Capsid protein p24: Virion (Potential).,Nucleocapsid protein p7: Virion (Potential).,Reverse transcriptase/ribonuclease H: Virion (Potential).,Integrase: Virion (Potential). Nucleus (Potential). Cytoplasm (Potential). Note=Nuclear at initial phase, cytoplasmic at assembly (Potential).Matrix protein p17: Virion (Potential). Nucleus (By similarity). Cytoplasm (By similarity). Cell membrane, Lipid-anchor (Potential). Note=Following virus entry, the nuclear localization signal (NLS) of the matrix protein participates with Vpr to the nuclear localization of the viral genome. During virus production, the nuclear export activity of the matrix protein counteracts the NLS to maintain the Gag and Gag-Pol polyproteins in the cytoplasm, thereby directing unspliced RNA to the plasma membrane (By similarity).,Capsid protein p24: Virion (Potential).,Nucleocapsid protein p7: Virion (Potential).,Reverse transcriptase/ribonuclease H: Virion (Potential).,Integrase: Virion (Potential). Nucleus (Potential). Cytoplasm (Potential). Note=Nuclear at initial phase, cytoplasmic at assembly (Potential).Matrix protein p17: Virion (Potential). Nucleus (By similarity). Cytoplasm (By similarity). Cell membrane, Lipid-anchor (Potential). Note=Following virus entry, the nuclear localization signal (NLS) of the matrix protein participates with Vpr to the nuclear localization of the viral genome. During virus production, the nuclear export activity of the matrix protein counteracts the NLS to maintain the Gag and Gag-Pol polyproteins in the cytoplasm, thereby directing unspliced RNA to the plasma membrane (By similarity).,Capsid protein p24: Virion (Potential).,Nucleocapsid protein p7: Virion (Potential).,Reverse transcriptase/ribonuclease H: Virion (Potential).,Integrase: Virion (Potential). Nucleus (Potential). Cytoplasm (Potential). Note=Nuclear at initial phase, cytoplasmic at assembly (Potential).Matrix protein p17: Virion (Potential). Nucleus (By similarity). Cytoplasm (By similarity). Cell membrane, Lipid-anchor (Potential). Note=Following virus entry, the nuclear localization signal (NLS) of the matrix protein participates with Vpr to the nuclear localization of the viral genome. During virus production, the nuclear export activity of the matrix protein counteracts the NLS to maintain the Gag and Gag-Pol polyproteins in the cytoplasm, thereby directing unspliced RNA to the plasma membrane (By similarity).,Capsid protein p24: Virion (Potential).,Nucleocapsid protein p7: Virion (Potential).,Reverse transcriptase/ribonuclease H: Virion (Potential).,Integrase: Virion (Potential). Nucleus (Potential). Cytoplasm (Potential). Note=Nuclear at initial phase, cytoplasmic at assembly (Potential).
CofactorBinds 2 magnesium ions for reverse transcriptase polymerase activity (By similarity).,Binds 2 magnesium ions for ribonuclease H (RNase H) activity. Substrate-binding is a precondition for magnesium binding (By similarity).,Magnesium ions for integrase activity. Binds at least 1, maybe 2 magnesium ions (By similarity).Binds 2 magnesium ions for reverse transcriptase polymerase activity (By similarity).,Binds 2 magnesium ions for ribonuclease H (RNase H) activity. Substrate-binding is a precondition for magnesium binding (By similarity).,Magnesium ions for integrase activity. Binds at least 1, maybe 2 magnesium ions (By similarity).Binds 2 magnesium ions for reverse transcriptase polymerase activity (By similarity).,Binds 2 magnesium ions for ribonuclease H (RNase H) activity. Substrate-binding is a precondition for magnesium binding (By similarity).,Magnesium ions for integrase activity. Binds at least 1, maybe 2 magnesium ions (By similarity).Binds 2 magnesium ions for reverse transcriptase polymerase activity (By similarity).,Binds 2 magnesium ions for ribonuclease H (RNase H) activity. Substrate-binding is a precondition for magnesium binding (By similarity).,Magnesium ions for integrase activity. Binds at least 1, maybe 2 magnesium ions (By similarity).

Compound table: links to PDB-related databases & PoSSuM

SubstratesProductsintermediates
KEGG-idC00017C00012C00001C00017C00012I00136
CompoundProteinPeptideH2OProteinPeptideAmino-diol-tetrahedral intermediate
Typepeptide/proteinpeptide/proteinH2Opeptide/proteinpeptide/protein
ChEBI

15377



PubChem

962
22247451



              
1a30AUnboundAnalogue:GLU-ASP-LEU UnboundUnboundUnbound
1ajvAUnboundUnbound UnboundUnboundTransition-state-analogue:NMB
1ajxAUnboundUnbound UnboundUnboundTransition-state-analogue:AH1
1axaAUnboundAnalogue:U0E-U0E UnboundUnboundUnbound
1bdlAUnboundUnbound UnboundAnalogue:IM1Unbound
1bdqAUnboundAnalogue:IM1 UnboundUnboundUnbound
1bdrAUnboundAnalogue:IM1 UnboundUnboundUnbound
1bv7AUnboundUnbound UnboundUnboundTransition-state-analogue:XV6
1bv9AUnboundUnbound UnboundUnboundTransition-state-analogue:XV6
1bveAUnboundUnbound UnboundUnboundTransition-state-analogue:DMP
1bvgAUnboundUnbound UnboundUnboundTransition-state-analogue:DMP
1bwaAUnboundUnbound UnboundUnboundTransition-state-analogue:XV6
1bwbAUnboundUnbound UnboundUnboundTransition-state-analogue:146
1d4hAUnboundUnbound UnboundUnboundTransition-state-analogue:BEH
1d4iAUnboundUnbound UnboundUnboundTransition-state-analogue:BEG
1d4jAUnboundUnbound UnboundUnboundTransition-state-analogue:MSC
1dmpAUnboundUnbound UnboundUnboundTransition-state-analogue:DMQ
1dw6CUnboundAnalogue:ARG-VAL-DCL-PHE-GLU-ALA-NLN UnboundUnboundUnbound
1ebkCUnboundAnalogue:ARG-VAL-DCL-PHE-GLU-ALA-NLN UnboundUnboundUnbound
1ebkEUnboundAnalogue:ARG-VAL-DCL-PHE-GLU-ALA-NLN UnboundUnboundUnbound
1ebwAUnboundUnbound UnboundUnboundTransition-state-analogue:BEI
1ebyAUnboundUnbound UnboundUnboundTransition-state-analogue:BEB
1ebzAUnboundUnbound UnboundUnboundTransition-state-analogue:BEC
1ec0AUnboundUnbound UnboundUnboundTransition-state-analogue:BED
1ec1AUnboundUnbound UnboundUnboundTransition-state-analogue:BEE
1ec2AUnboundUnbound UnboundUnboundTransition-state-analogue:BEJ
1ec3AUnboundUnbound UnboundUnboundTransition-state-analogue:MS3
1fejCUnboundAnalogue:ACE-THR-ILE-NLE-NLE-GLN-ARG UnboundUnboundUnbound
1ff0CUnboundAnalogue:ACE-THR-ILE-NLE-NLE-GLN-ARG UnboundUnboundUnbound
1fffCUnboundAnalogue:ARG-VAL-DCL-PHE-GLU-ALA-NLE-NH2 UnboundUnboundUnbound
1ffiCUnboundAnalogue:ACE-THR-ILE-NLE-NLE-GLN-ARG UnboundUnboundUnbound
1fg6CUnboundAnalogue:ACE-THR-ILE-NLE-NLE-GLN-ARG UnboundUnboundUnbound
1fg8CUnboundAnalogue:ARG-VAL-DCL-PHE-GLU-ALA-NLE-NH2 UnboundUnboundUnbound
1fgcCUnboundAnalogue:ACE-THR-ILE-NLE-NLE-GLN-ARG UnboundUnboundUnbound
1g2kAUnboundUnbound UnboundUnboundTransition-state-analogue:NM1
1g6lA01UnboundUnbound UnboundUnboundUnbound
1gnnAUnboundAnalogue:U0E-U0E UnboundUnboundUnbound
1gnoAUnboundAnalogue:U0E-U0E UnboundUnboundUnbound
1hbvAUnboundAnalogue:GAN UnboundUnboundUnbound
1hefEUnboundAnalogue:ALA-ALA-PHE-OHE-PHE-VAL-VAL-OME UnboundUnboundUnbound
1hegEUnboundAnalogue:ALA-ALA-PHE-OHE-GLY-VAL-VAL-OME UnboundUnboundUnbound
1hihAUnboundAnalogue:C20 UnboundUnboundUnbound
1hivAUnboundAnalogue:NOA-HIS-CAV-ILE-APY UnboundUnboundUnbound
1hosAUnboundUnbound UnboundUnboundTransition-state-analogue:PHP
1hpsAUnboundAnalogue:RUN-RUN UnboundUnboundUnbound
1hpvAUnboundAnalogue:478 UnboundUnboundUnbound
1hteAUnboundUnbound Bound:LEU-GLN-GLU-SERAnalogue:G23Unbound
1htfAUnboundUnbound Analogue:G26UnboundUnbound
1htgAUnboundAnalogue:G37 UnboundUnboundUnbound
1hvhAUnboundUnbound UnboundUnboundTransition-state-analogue:Q82
1hviAUnboundUnbound UnboundUnboundTransition-state-analogue:A77
1hvjAUnboundAnalogue:A78 UnboundUnboundUnbound
1hvkAUnboundUnbound UnboundUnboundTransition-state-analogue:A79
1hvlAUnboundUnbound UnboundUnboundTransition-state-analogue:A76
1hvrAUnboundUnbound UnboundUnboundTransition-state-analogue:XK2
1hvsAUnboundUnbound UnboundUnboundTransition-state-analogue:A77
1hwrAUnboundUnbound UnboundUnboundTransition-state-analogue:216
1hxbAUnboundAnalogue:QNC-ASN-HPH-DIQ-NTB UnboundUnboundUnbound
1k1tAUnboundAnalogue:ARG-VAL-DCL-PHE-GLU-ALA-NLE UnboundUnboundUnbound
1k1uAUnboundAnalogue:ARG-VAL-DCL-PHE-GLU-ALA-NLE UnboundUnboundUnbound
1k2bAUnboundAnalogue:ARG-VAL-DCL-PHE-GLU-ALA-NLE-NH2 UnboundUnboundUnbound
1k2cAUnboundAnalogue:ARG-VAL-DCL-PHE-GLU-ALA-NLE-NH2 UnboundUnboundUnbound
1k6cAUnboundAnalogue:MK1 UnboundUnboundUnbound
1k6pAUnboundAnalogue:XN3 UnboundUnboundUnbound
1k6tAUnboundAnalogue:XN1 UnboundUnboundUnbound
1k6vAUnboundAnalogue:XN2 UnboundUnboundUnbound
1lv1A01UnboundUnbound UnboundUnboundUnbound
1merAUnboundUnbound UnboundUnboundTransition-state-analogue:DMQ
1mesAUnboundUnbound UnboundUnboundTransition-state-analogue:DMP
1metAUnboundUnbound UnboundUnboundTransition-state-analogue:DMP
1meuAUnboundUnbound UnboundUnboundTransition-state-analogue:DMP
1odwAUnboundAnalogue:BOC-HPH-DMN-HPH-BOC UnboundUnboundUnbound
1odxAUnboundAnalogue:BOC-HPH-DMN-HPH-BOC UnboundUnboundUnbound
1odyAUnboundAnalogue:LP1 UnboundUnboundUnbound
1qbrAUnboundUnbound UnboundUnboundTransition-state-analogue:XV6
1qbsAUnboundUnbound UnboundUnboundTransition-state-analogue:DMP
1qbtAUnboundUnbound UnboundUnboundTransition-state-analogue:146
1qbuAUnboundUnbound UnboundUnboundTransition-state-analogue:846
1sbgAUnboundAnalogue:IM1 UnboundUnboundUnbound
1tcxAUnboundAnalogue:IM1 UnboundUnboundUnbound
2bpvAUnboundAnalogue:1IN UnboundUnboundUnbound
2bpwAUnboundAnalogue:1IN UnboundUnboundUnbound
2bpxAUnboundAnalogue:MK1 UnboundUnboundUnbound
2bpyAUnboundAnalogue:3IN UnboundUnboundUnbound
2bpzAUnboundAnalogue:3IN UnboundUnboundUnbound
3phvAUnboundUnbound UnboundUnboundUnbound
3tlhAUnboundAnalogue:INT UnboundUnboundUnbound
9hvpAUnboundAnalogue:PHQ-VAL-COR-VAL-PHQ UnboundUnboundUnbound
1a30BUnboundUnbound UnboundUnboundUnbound
1ajvBUnboundUnbound UnboundUnboundUnbound
1ajxBUnboundUnbound UnboundUnboundUnbound
1axaBUnboundUnbound UnboundUnboundUnbound
1bdlBUnboundUnbound UnboundAnalogue:IM1Unbound
1bdqBUnboundUnbound UnboundUnboundUnbound
1bdrBUnboundUnbound UnboundUnboundUnbound
1bv7BUnboundUnbound UnboundUnboundUnbound
1bv9BUnboundUnbound UnboundUnboundUnbound
1bveBUnboundUnbound UnboundUnboundUnbound
1bvgBUnboundUnbound UnboundUnboundUnbound
1bwaBUnboundUnbound UnboundUnboundUnbound
1bwbBUnboundUnbound UnboundUnboundUnbound
1d4hBUnboundUnbound UnboundUnboundUnbound
1d4iBUnboundUnbound UnboundUnboundUnbound
1d4jBUnboundUnbound UnboundUnboundUnbound
1dmpBUnboundUnbound UnboundUnboundUnbound
1dw6DUnboundUnbound UnboundUnboundUnbound
1ebkDUnboundUnbound UnboundUnboundUnbound
1ebkFUnboundUnbound UnboundUnboundUnbound
1ebwBUnboundUnbound UnboundUnboundUnbound
1ebyBUnboundUnbound UnboundUnboundUnbound
1ebzBUnboundUnbound UnboundUnboundUnbound
1ec0BUnboundUnbound UnboundUnboundUnbound
1ec1BUnboundUnbound UnboundUnboundUnbound
1ec2BUnboundUnbound UnboundUnboundUnbound
1ec3BUnboundUnbound UnboundUnboundUnbound
1fejDUnboundUnbound UnboundUnboundUnbound
1ff0DUnboundUnbound UnboundUnboundUnbound
1fffDUnboundUnbound UnboundUnboundUnbound
1ffiDUnboundUnbound UnboundUnboundUnbound
1fg6DUnboundUnbound UnboundUnboundUnbound
1fg8DUnboundUnbound UnboundUnboundUnbound
1fgcDUnboundUnbound UnboundUnboundUnbound
1g2kBUnboundUnbound UnboundUnboundUnbound
1g6lA02UnboundUnbound UnboundUnboundUnbound
1gnnBUnboundUnbound UnboundUnboundUnbound
1gnoBUnboundUnbound UnboundUnboundUnbound
1hbvBUnboundUnbound UnboundUnboundUnbound
1hihBUnboundUnbound UnboundUnboundUnbound
1hivBUnboundUnbound UnboundUnboundUnbound
1hosBUnboundUnbound UnboundUnboundUnbound
1hpsBUnboundUnbound UnboundUnboundUnbound
1hpvBUnboundUnbound UnboundUnboundUnbound
1hteBUnboundUnbound UnboundUnboundUnbound
1htfBUnboundUnbound UnboundUnboundUnbound
1htgBUnboundUnbound UnboundUnboundUnbound
1hvhBUnboundUnbound UnboundUnboundUnbound
1hviBUnboundUnbound UnboundUnboundUnbound
1hvjBUnboundUnbound UnboundUnboundUnbound
1hvkBUnboundUnbound UnboundUnboundUnbound
1hvlBUnboundUnbound UnboundUnboundUnbound
1hvrBUnboundUnbound UnboundUnboundUnbound
1hvsBUnboundUnbound UnboundUnboundUnbound
1hwrBUnboundUnbound UnboundUnboundUnbound
1hxbBUnboundUnbound UnboundUnboundUnbound
1k1tBUnboundUnbound UnboundUnboundUnbound
1k1uBUnboundUnbound UnboundUnboundUnbound
1k2bBUnboundUnbound UnboundUnboundUnbound
1k2cBUnboundUnbound UnboundUnboundUnbound
1k6cBUnboundUnbound UnboundUnboundUnbound
1k6pBUnboundUnbound UnboundUnboundUnbound
1k6tBUnboundUnbound UnboundUnboundUnbound
1k6vBUnboundUnbound UnboundUnboundUnbound
1lv1A02UnboundUnbound UnboundUnboundUnbound
1merBUnboundUnbound UnboundUnboundUnbound
1mesBUnboundUnbound UnboundUnboundUnbound
1metBUnboundUnbound UnboundUnboundUnbound
1meuBUnboundUnbound UnboundUnboundUnbound
1odwBUnboundUnbound UnboundUnboundUnbound
1odxBUnboundUnbound UnboundUnboundUnbound
1odyBUnboundUnbound UnboundUnboundUnbound
1qbrBUnboundUnbound UnboundUnboundUnbound
1qbsBUnboundUnbound UnboundUnboundUnbound
1qbtBUnboundUnbound UnboundUnboundUnbound
1qbuBUnboundUnbound UnboundUnboundUnbound
1sbgBUnboundUnbound UnboundUnboundUnbound
1tcxBUnboundUnbound UnboundUnboundUnbound
2bpvBUnboundUnbound UnboundUnboundUnbound
2bpwBUnboundUnbound UnboundUnboundUnbound
2bpxBUnboundUnbound UnboundUnboundUnbound
2bpyBUnboundUnbound UnboundUnboundUnbound
2bpzBUnboundUnbound UnboundUnboundUnbound
9hvpBUnboundUnbound UnboundUnboundUnbound

Active-site residues
resource
Swiss-prot;P35963
pdbCatalytic residuescomment
          
1a30AASP   25
 
1ajvAASP   25
 
1ajxAASP   25
 
1axaAASP   25
mutant A28S
1bdlAASP   25
mutant T31S, V32I, L33V, E34A, E35G, M36I, S37E
1bdqAASP   25
mutant T31S, V32I, L33V, E34A, E35G, M36I, S37E, I47V, V82I
1bdrAASP   25
mutant T31S, L33V, E34T, E35G, M36I, S37E
1bv7AASP   25
 
1bv9AASP   25
mutant I84V
1bveAASP   25
mutant C95A
1bvgAASP   25
mutant C95A
1bwaAASP   25
mutant V82F, I84V
1bwbAASP   25
mutant V82F, I84V
1d4hAASP   25
 
1d4iAASP   25
 
1d4jAASP   25
 
1dmpAASP   25
 
1dw6CASP   25
mutant Q7K, L33I, L63I, C67A, L90M, C95A
1ebkCASP   25
mutant Q7K, R8Q, L33I, L63I, C67A, C95A
1ebkEASP   25
mutant Q7K, R8Q, L33I, L63I, C67A, C95A
1ebwAASP   25
 
1ebyAASP   25
 
1ebzAASP   25
 
1ec0AASP   25
 
1ec1AASP   25
 
1ec2AASP   25
 
1ec3AASP   25
 
1fejCASP   25
mutant L90M
1ff0CASP   25
mutant K45I
1fffCASP   25
mutant D30N
1ffiCASP   25
mutant D30N
1fg6CASP   25
mutant N88D
1fg8CASP   25
mutant N88D
1fgcCASP   25
 
1g2kAASP   25
 
1g6lA01ASP   25
 
1gnnAASP   25
mutant V82N
1gnoAASP   25
 
1hbvAASP   25
 
1hefEASP   25
 
1hegEASP   25
 
1hihAASP   25
 
1hivAASP   25
 
1hosAASP   25
 
1hpsAASP   25
 
1hpvAASP   25
 
1hteAASP   25
 
1htfAASP   25
 
1htgAASP   25
 
1hvhAASP   25
 
1hviAASP   25
 
1hvjAASP   25
 
1hvkAASP   25
 
1hvlAASP   25
 
1hvrAASP   25
 
1hvsAASP   25
mutant V82A
1hwrAASP   25
 
1hxbAASP   25
 
1k1tAASP   25
mutant K45I, V82S
1k1uAASP   25
mutant K45I, L90M
1k2bAASP   25
mutant N88D, L90M
1k2cAASP   25
mutant D30N, V82S
1k6cAASP   25
mutant Q7K, K14R, V82T, I84V
1k6pAASP   25
mutant Q7K, K14R, V82T, I84V
1k6tAASP   25
mutant Q7K, K14R, V82T, I84V
1k6vAASP   25
mutant Q7K, K14R, V82T, I84V
1lv1A01ASP   25
mutant C95M
1merAASP   25
mutant I84V
1mesAASP   25
mutant I84V
1metAASP   25
mutant V82F
1meuAASP   25
mutant V82F, I84V
1odwAASP   25
 
1odxAASP   25
mutant A71T, V82A
1odyAASP   25
 
1qbrAASP   25
 
1qbsAASP   25
 
1qbtAASP   25
 
1qbuAASP   25
 
1sbgAASP   25
 
1tcxAASP   25
mutant I32V, V47I, I82V
2bpvAASP   25
 
2bpwAASP   25
 
2bpxAASP   25
 
2bpyAASP   25
 
2bpzAASP   25
 
3phvAASP   25
 
3tlhAASP   25
 
9hvpAASP   25
 
1a30BASP   25
 
1ajvBASP   25
 
1ajxBASP   25
 
1axaBASP   25
mutant A28S
1bdlBASP   25
mutant T31S, V32I, L33V, E34A, E35G, M36I, S37E
1bdqBASP   25
mutant T31S, V32I, L33V, E34A, E35G, M36I, S37E, I47V, V82I
1bdrBASP   25
mutant T31S, L33V, E34T, E35G, M36I, S37E
1bv7BASP   25
 
1bv9BASP   25
mutant I84V
1bveBASP   25
mutant C95A
1bvgBASP   25
mutant C95A
1bwaBASP   25
mutant V82F, I84V
1bwbBASP   25
mutant V82F, I84V
1d4hBASP  125
 
1d4iBASP  125
 
1d4jBASP  125
 
1dmpBASP   25
 
1dw6DASP  125
mutant Q107K, L133I, L163I, C167A, L190M, C195A
1ebkDASP  125
mutant Q107K, R108Q, L133I, L163I, C167A, C195A
1ebkFASP  125
mutant Q107K, R108Q, L133I, L163I, C167A, C195A
1ebwBASP  125
 
1ebyBASP  125
 
1ebzBASP  125
 
1ec0BASP  125
 
1ec1BASP  125
 
1ec2BASP  125
 
1ec3BASP  125
 
1fejDASP  125
mutant L190M
1ff0DASP  125
mutant K145I
1fffDASP  125
mutant D130N
1ffiDASP  125
mutant D130N
1fg6DASP  125
mutant N188D
1fg8DASP  125
mutant N188D
1fgcDASP  125
 
1g2kBASP   25
 
1g6lA02ASP 1025
 
1gnnBASP   25
mutant V82N
1gnoBASP   25
 
1hbvBASP   25
 
1hihBASP   25
 
1hivBASP   25
 
1hosBASP   25
 
1hpsBASP   25
 
1hpvBASP   25
 
1hteBASP   25
 
1htfBASP   25
 
1htgBASP   25
 
1hvhBASP   25
 
1hviBASP   25
 
1hvjBASP   25
 
1hvkBASP   25
 
1hvlBASP   25
 
1hvrBASP   25
 
1hvsBASP   25
mutant V82A
1hwrBASP   25
 
1hxbBASP   25
 
1k1tBASP  125
mutant K145I, V182S
1k1uBASP  125
mutant K145I, L190M
1k2bBASP   25
mutant N88D, L90M
1k2cBASP   25
mutant D30N, V82S
1k6cBASP   25
mutant Q7K, K14R, V82T, I84V
1k6pBASP   25
mutant Q7K, K14R, V82T, I84V
1k6tBASP   25
mutant Q7K, K14R, V82T, I84V
1k6vBASP   25
mutant Q7K,K14R,V82T,I84V
1lv1A02ASP 1025
mutant C1095A
1merBASP   25
mutant I84V
1mesBASP   25
mutant I84V
1metBASP   25
mutant V82F
1meuBASP   25
mutant V82F, I84V
1odwBASP   25
 
1odxBASP   25
mutant A71T, V82A
1odyBASP   25
 
1qbrBASP   25
 
1qbsBASP   25
 
1qbtBASP   25
 
1qbuBASP   25
 
1sbgBASP   25
 
1tcxBASP   25
mutant I32V, V47I, I82V
2bpvBASP   25
 
2bpwBASP   25
 
2bpxBASP   25
 
2bpyBASP   25
 
2bpzBASP   25
 
9hvpBASP   25
 

References for Catalytic Mechanism
ReferencesSectionsNo. of steps in catalysis
[1]p.302
[7]Fig.4, p.8461-8462
[8]p.1607-1608
[9]Fig.5, p.24363-24365
[14]p.7978-7979
[33]Fig.7, p.12942-12943
[39]Fig.17, p.336-339
[40]p.949
[42]p.682
[79]Fig.8, p.803
[81]Fig.1
[100]Fig.2

references
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TitleX-ray analysis of HIV-1 proteinase at 2.7 A resolution confirms structural homology among retroviral enzymes.
Related PDB3phv
Related UniProtKBP03366
[2]
Comments3D-STRUCTURE MODELING OF PROTEASE DOMAIN.
Medline ID89146134
PubMed ID2537531
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Related UniProtKBP03366
[3]
PubMed ID2201682
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Year1990
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Pages14209-19
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Related PDB9hvp
Related UniProtKBP03366
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PubMed ID1812742
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Year1991
Volume306
Pages455-60
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PubMed ID1993177
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Year1991
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Pages1600-9
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[9]
PubMed ID1761538
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Year1991
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Pages24359-66
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TitleKinetic studies of human immunodeficiency virus type 1 protease and its active-site hydrogen bond mutant A28S.
[10]
CommentsX-ray crystallography
PubMed ID1956054
JournalJ Med Chem
Year1991
Volume34
Pages3340-2
AuthorsKrohn A, Redshaw S, Ritchie JC, Graves BJ, Hatada MH
TitleNovel binding mode of highly potent HIV-proteinase inhibitors incorporating the (R)-hydroxyethylamine isostere.
Related PDB1hxb
[11]
CommentsX-ray crystallography
PubMed ID1429626
JournalJ Biol Chem
Year1992
Volume267
Pages22770-8
AuthorsMurthy KH, Winborne EL, Minnich MD, Culp JS, Debouck C
TitleThe crystal structures at 2.2-A resolution of hydroxyethylene-based inhibitors bound to human immunodeficiency virus type 1 protease show that the inhibitors are present in two distinct orientations.
Related PDB1heg
[12]
CommentsX-ray crystallography
PubMed ID1304383
JournalProtein Sci
Year1992
Volume1
Pages1061-72
AuthorsThanki N, Rao JK, Foundling SI, Howe WJ, Moon JB, Hui JO, Tomasselli AG, Heinrikson RL, Thaisrivongs S, Wlodawer A
TitleCrystal structure of a complex of HIV-1 protease with a dihydroxyethylene-containing inhibitor: comparisons with molecular modeling.
Related PDB1hiv
[13]
PubMed ID8352596
JournalAnnu Rev Biochem
Year1993
Volume62
Pages543-85
AuthorsWlodawer A, Erickson JW
TitleStructure-based inhibitors of HIV-1 protease.
[14]
CommentsX-ray crystallography
PubMed ID8347601
JournalBiochemistry
Year1993
Volume32
Pages7972-80
AuthorsAbdel-Meguid SS, Zhao B, Murthy KH, Winborne E, Choi JK, DesJarlais RL, Minnich MD, Culp JS, Debouck C, Tomaszek TA Jr, et al
TitleInhibition of human immunodeficiency virus-1 protease by a C2-symmetric phosphinate. Synthesis and crystallographic analysis.
Related PDB1hos
[15]
CommentsX-ray crystallography
PubMed ID7918383
JournalBiochemistry
Year1994
Volume33
Pages11671-7
AuthorsAbdel-Meguid SS, Metcalf BW, Carr TJ, Demarsh P, DesJarlais RL, Fisher S, Green DW, Ivanoff L, Lambert DM, Murthy KH, et al
TitleAn orally bioavailable HIV-1 protease inhibitor containing an imidazole-derived peptide bond replacement: crystallographic and pharmacokinetic analysis.
Related PDB1sbg
[16]
CommentsX-ray crystallography
PubMed ID8031777
JournalBiochemistry
Year1994
Volume33
Pages8417-27
AuthorsJhoti H, Singh OM, Weir MP, Cooke R, Murray-Rust P, Wonacott A
TitleX-ray crystallographic studies of a series of penicillin-derived asymmetric inhibitors of HIV-1 protease.
Related PDB1hte,1htf,1htg
[17]
CommentsX-ray crystallography
JournalJ Am Chem Soc
Year1994
Volume116
Pages847-55
AuthorsHosur MV, Bhat TN, Kempf DJ, Baldwin ET, Liu B, Gulnik S, Wideburg NE, Norbeck DW, Appelt K, Erickson JW
TitleInfluence of stereochemistry on activity and binding modes for C2 symmetry-based diol inhibitors of HIV-1 protease.
Related PDB1hvi,1hvj,1hvk,1hvl
[18]
CommentsX-ray crystallography
PubMed ID7932533
JournalJ Med Chem
Year1994
Volume37
Pages3100-7
AuthorsThompson SK, Murthy KH, Zhao B, Winborne E, Green DW, Fisher SM, DesJarlais RL, Tomaszek TA Jr, Meek TD, Gleason JG, et al
TitleRational design, synthesis, and crystallographic analysis of a hydroxyethylene-based HIV-1 protease inhibitor containing a heterocyclic P1'--P2' amide bond isostere.
Related PDB1hps
[19]
CommentsX-ray crystallography
PubMed ID8278812
JournalScience
Year1994
Volume263
Pages380-4
AuthorsLam PY, Jadhav PK, Eyermann CJ, Hodge CN, Ru Y, Bacheler LT, Meek JL, Otto MJ, Rayner MM, Wong YN, et al
TitleRational design of potent, bioavailable, nonpeptide cyclic ureas as HIV protease inhibitors.
Related PDB1hvr
[20]
PubMed ID8540354
JournalAdv Exp Med Biol
Year1995
Volume362
Pages439-44
AuthorsBhat TN, Baldwin ET, Liu B, Cheng YS, Erickson JW
TitleX-ray structure of a tethered dimer for HIV-1 protease.
[21]
PubMed ID8540357
JournalAdv Exp Med Biol
Year1995
Volume362
Pages455-60
AuthorsCollins JR, Burt SK, Erickson JW
TitleActivated dynamics of flap opening in HIV-1 protease.
[22]
PubMed ID8540356
JournalAdv Exp Med Biol
Year1995
Volume362
Pages451-4
AuthorsSilva AM, Cachau RE, Baldwin ET, Gulnik S, Sham HL, Erickson JW
TitleMolecular dynamics of HIV-1 protease in complex with a difluoroketone-containing inhibitor: implications for the catalytic mechanism.
[23]
PubMed ID9383433
JournalChem Biol
Year1995
Volume2
Pages317-24
AuthorsGehlhaar DK, Verkhivker GM, Rejto PA, Sherman CJ, Fogel DB, Fogel LJ, Freer ST
TitleMolecular recognition of the inhibitor AG-1343 by HIV-1 protease: conformationally flexible docking by evolutionary programming.
[24]
CommentsX-ray crystallography
JournalJ Am Chem Soc
Year1995
Volume117
Pages1181-2
AuthorsKim E.E, Baker CT, Dwyer MD, Murcko MA, Rao BG, Tung RD, Navia MA
TitleCrystal structure of HIV-1 protease in complex with VX-478, a potent and orally bioavailable inhibitor of the enzyme.
Related PDB1hpv
[25]
PubMed ID7665551
JournalJ Biol Chem
Year1995
Volume270
Pages21433-6
AuthorsChen Z, Li Y, Schock HB, Hall D, Chen E, Kuo LC
TitleThree-dimensional structure of a mutant HIV-1 protease displaying cross-resistance to all protease inhibitors in clinical trials.
[26]
CommentsX-ray crystallography
PubMed ID7650677
JournalJ Med Chem
Year1995
Volume38
Pages3246-52
AuthorsHoog SS, Zhao B, Winborne E, Fisher S, Green DW, DesJarlais RL, Newlander KA, Callahan JF, Moore ML, Huffman WF, et al
TitleA check on rational drug design: crystal structure of a complex of human immunodeficiency virus type 1 protease with a novel gamma-turn mimetic inhibitor.
Related PDB1hef
[27]
PubMed ID7796263
JournalNat Struct Biol
Year1995
Volume2
Pages274-80
AuthorsNicholson LK, Yamazaki T, Torchia DA, Grzesiek S, Bax A, Stahl SJ, Kaufman JD, Wingfield PT, Lam PY, Jadhav PK, et al
TitleFlexibility and function in HIV-1 protease.
[28]
PubMed ID8590019
JournalStructure
Year1995
Volume3
Pages581-90
AuthorsBaldwin ET, Bhat TN, Gulnik S, Liu B, Topol IA, Kiso Y, Mimoto T, Mitsuya H, Erickson JW
TitleStructure of HIV-1 protease with KNI-272, a tight-binding transition-state analog containing allophenylnorstatine.
[29]
CommentsX-ray crystallography
PubMed ID7613867
JournalStructure
Year1995
Volume3
Pages381-9
AuthorsPriestle JP, Fassler A, Rosel J, Tintelnot-Blomley M, Strop P, Grutter MG
TitleComparative analysis of the X-ray structures of HIV-1 and HIV-2 proteases in complex with CGP 53820, a novel pseudosymmetric inhibitor.
Related PDB1hih
[30]
PubMed ID8652592
JournalBiochemistry
Year1996
Volume35
Pages2482-8
AuthorsDavis DA, Dorsey K, Wingfield PT, Stahl SJ, Kaufman J, Fales HM, Levine RL
TitleRegulation of HIV-1 protease activity through cysteine modification.
[31]
CommentsX-ray crystallography
PubMed ID8718851
JournalBiochemistry
Year1996
Volume35
Pages10627-33
AuthorsHong L, Treharne A, Hartsuck JA, Foundling S, Tang J
TitleCrystal structures of complexes of a peptidic inhibitor with wild-type and two mutant HIV-1 proteases.
Related PDB1gnn,1gno
[32]
CommentsX-ray crystallography
PubMed ID8756683
JournalBiochemistry
Year1996
Volume35
Pages10279-86
AuthorsHoog SS, Towler EM, Zhao B, Doyle ML, Debouck C, Abdel-Meguid SS
TitleHuman immunodeficiency virus protease ligand specificity conferred by residues outside of the active site cavity.
Related PDB1tcx
[33]
PubMed ID8841139
JournalBiochemistry
Year1996
Volume35
Pages12933-44
AuthorsRose RB, Craik CS, Douglas NL, Stroud RM
TitleThree-dimensional structures of HIV-1 and SIV protease product complexes.
[34]
PubMed ID8756455
JournalBiochemistry
Year1996
Volume35
Pages9945-50
AuthorsWang YX, Freedberg DI, Yamazaki T, Wingfield PT, Stahl SJ, Kaufman JD, Kiso Y, Torchia DA
TitleSolution NMR evidence that the HIV-1 protease catalytic aspartyl groups have different ionization states in the complex formed with the asymmetric drug KNI-272.
[35]
CommentsX-ray crystallography
PubMed ID8807858
JournalChem Biol
Year1996
Volume3
Pages301-14
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TitleImproved cyclic urea inhibitors of the HIV-1 protease: synthesis, potency, resistance profile, human pharmacokinetics and X-ray crystal structure of DMP 450.
Related PDB1dmp
[36]
PubMed ID8621402
JournalJ Biol Chem
Year1996
Volume271
Pages5458-63
AuthorsSzeltner Z, Polgar L
TitleConformational stability and catalytic activity of HIV-1 protease are both enhanced at high salt concentration.
[37]
CommentsX-ray crystallography
PubMed ID8784449
JournalJ Med Chem
Year1996
Volume39
Pages3514-25
AuthorsLam PY, Ru Y, Jadhav PK, Aldrich PE, DeLucca GV, Eyermann CJ, Chang CH, Emmett G, Holler ER, Daneker WF, Li L, Confalone PN, McHugh RJ, Han Q, Li R, Markwalder JA, Seitz SP, Sharpe TR, Bacheler LT, Rayner MM, Klabe RM, Shum L, Winslow DL, Kornhauser DM, Hodge CN, et al
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Related PDB1qbs
[38]
PubMed ID8667359
JournalJ Med Chem
Year1996
Volume39
Pages2156-69
AuthorsNugiel DA, Jacobs K, Kaltenbach RF, Worley T, Patel M, Meyer DT, Jadhav PK, De Lucca GV, Smyser TE, Klabe RM, Bacheler LT, Rayner MM, Seitz SP
TitlePreparation and structure-activity relationship of novel P1/P1'-substituted cyclic urea-based human immunodeficiency virus type-1 protease inhibitors.
[39]
PubMed ID8551523
JournalJ Mol Biol
Year1996
Volume255
Pages321-46
AuthorsSilva AM, Cachau RE, Sham HL, Erickson JW
TitleInhibition and catalytic mechanism of HIV-1 aspartic protease.
[40]
PubMed ID8901873
JournalNat Struct Biol
Year1996
Volume3
Pages946-50
AuthorsSmith R, Brereton IM, Chai RY, Kent SB
TitleIonization states of the catalytic residues in HIV-1 protease.
[41]
PubMed ID9390264
JournalPac Symp Biocomput
Year1996
Volume
Pages638-52
AuthorsVerkhivker GM
TitleEmpirical free energy calculations of human immunodeficiency virus type 1 protease crystallographic complexes. II. Knowledge-based ligand-protein interaction potentials applied to thermodynamic analysis of hydrophobic mutations.
[42]
PubMed ID8875645
JournalProtein Eng
Year1996
Volume9
Pages679-90
AuthorsWeber IT, Harrison RW
TitleMolecular mechanics calculations on HIV-1 protease with peptide substrates correlate with experimental data.
[43]
CommentsX-ray crystallography
JournalProtein Pept Lett
Year1996
Volume3
Pages399-406
AuthorsKervinen J, Thanki N, Zdanov A, Tino J, Barrish J, Pin FL, Colonno R, Riccardi K, Samanta H, Wlodawer A
TitleStructural Analysis of the Native and Drug-Resistant HIV-1 Proteinases Complexed with an Aminodiol Inhibitor.
Related PDB1odx
[44]
CommentsSTRUCTURE BY NMR OF 57-155.
Medline ID97022126
PubMed ID8868486
JournalProtein Sci
Year1996
Volume5
Pages495-506
AuthorsYamazaki T, Hinck AP, Wang YX, Nicholson LK, Torchia DA, Wingfield P, Stahl SJ, Kaufman JD, Chang CH, Domaille PJ, Lam PY
TitleThree-dimensional solution structure of the HIV-1 protease complexed with DMP323, a novel cyclic urea-type inhibitor, determined by nuclear magnetic resonance spectroscopy.
Related PDB1bve,1bvg
Related UniProtKBP04585
[45]
CommentsX-ray crystallography
PubMed ID9048541
JournalBiochemistry
Year1997
Volume36
Pages1573-80
AuthorsAla PJ, Huston EE, Klabe RM, McCabe DD, Duke JL, Rizzo CJ, Korant BD, DeLoskey RJ, Lam PY, Hodge CN, Chang CH
TitleMolecular basis of HIV-1 protease drug resistance: structural analysis of mutant proteases complexed with cyclic urea inhibitors.
Related PDB1mer,1mes,1met,1meu
[46]
PubMed ID9346283
JournalEur J Biochem
Year1997
Volume248
Pages313-22
AuthorsLange-Savage G, Berchtold H, Liesum A, Budt KH, Peyman A, Knolle J, Sedlacek J, Fabry M, Hilgenfeld R
TitleStructure of HOE/BAY 793 complexed to human immunodeficiency virus (HIV-1) protease in two different crystal forms--structure/function relationship and influence of crystal packing.
[47]
PubMed ID9188447
JournalJ Biol Chem
Year1997
Volume272
Pages15603-6
AuthorsVance JE, LeBlanc DA, Wingfield P, London RE
TitleConformational selectivity of HIV-1 protease cleavage of X-Pro peptide bonds and its implications.
[48]
CommentsX-ray crystallography
PubMed ID9083478
JournalJ Med Chem
Year1997
Volume40
Pages898-902
AuthorsBackbro K, Lowgren S, Osterlund K, Atepo J, Unge T, Hulten J, Bonham NM, Schaal W, Karlen A, Hallberg A
TitleUnexpected binding mode of a cyclic sulfamide HIV-1 protease inhibitor.
Related PDB1ajv,1ajx
[49]
CommentsX-ray crystallography
PubMed ID9003516
JournalJ Med Chem
Year1997
Volume40
Pages181-91
AuthorsJadhav PK, Ala P, Woerner FJ, Chang CH, Garber SS, Anton ED, Bacheler LT
TitleCyclic urea amides: HIV-1 protease inhibitors with low nanomolar potency against both wild type and protease inhibitor resistant mutants of HIV.
Related PDB1qbr,1qbt,1qbu
[50]
PubMed ID9258349
JournalJ Med Chem
Year1997
Volume40
Pages2440-4
AuthorsSmith AB 3rd, Hirschmann R, Pasternak A, Yao W, Sprengeler PA, Holloway MK, Kuo LC, Chen Z, Darke PL, Schleif WA
TitleAn orally bioavailable pyrrolinone inhibitor of HIV-1 protease: computational analysis and X-ray crystal structure of the enzyme complex.
[51]
PubMed ID9061782
JournalProteins
Year1997
Volume27
Pages184-94
AuthorsMiller M, Geller M, Gribskov M, Kent SB
TitleAnalysis of the structure of chemically synthesized HIV-1 protease complexed with a hexapeptide inhibitor. Part I: Crystallographic refinement of 2 A data.
[52]
CommentsX-ray crystallography
PubMed ID9757136
JournalActa Crystallogr D Biol Crystallogr
Year1998
Volume54
Pages1053-60
AuthorsMunshi S, Chen Z, Li Y, Olsen DB, Fraley ME, Hungate RW, Kuo LC
TitleRapid X-ray diffraction analysis of HIV-1 protease-inhibitor complexes: inhibitor exchange in single crystals of the bound enzyme.
Related PDB2bpv,2bpw,2bpx,2bpy,2bpz
[53]
PubMed ID9561200
JournalAdv Exp Med Biol
Year1998
Volume436
Pages59-63
AuthorsHong L, Zhang C, Hartsuck JA, Foundling S, Tang J
TitleX-ray crystallographic studies of the structure-function relationships of HIV-1 protease.
[54]
CommentsX-ray crystallography
PubMed ID9790666
JournalBiochemistry
Year1998
Volume37
Pages15042-9
AuthorsAla PJ, Huston EE, Klabe RM, Jadhav PK, Lam PY, Chang CH
TitleCounteracting HIV-1 protease drug resistance: structural analysis of mutant proteases complexed with XV638 and SD146, cyclic urea amides with broad specificities.
Related PDB1bv7,1bv9,1bwa,1bwb
[55]
CommentsX-ray crystallography
PubMed ID9485357
JournalBiochemistry
Year1998
Volume37
Pages2105-10
AuthorsLouis JM, Dyda F, Nashed NT, Kimmel AR, Davies DR
TitleHydrophilic peptides derived from the transframe region of Gag-Pol inhibit the HIV-1 protease.
Related PDB1a30
[56]
CommentsX-ray crystallography
PubMed ID9692985
JournalBiochemistry
Year1998
Volume37
Pages10928-36
AuthorsSwairjo MA, Towler EM, Debouck C, Abdel-Meguid SS
TitleStructural role of the 30's loop in determining the ligand specificity of the human immunodeficiency virus protease.
Related PDB1bdr
[57]
PubMed ID9860826
JournalBiochemistry
Year1998
Volume37
Pages17137-44
AuthorsTowler EM, Gulnik SV, Bhat TN, Xie D, Gustschina E, Sumpter TR, Robertson N, Jones C, Sauter M, Mueller-Lantzsch N, Debouck C, Erickson JW
TitleFunctional characterization of the protease of human endogenous retrovirus, K10: can it complement HIV-1 protease?
[58]
PubMed ID9881109
JournalBioorg Med Chem
Year1998
Volume6
Pages2185-92
AuthorsGupta SP, Babu MS, Sowmya S
TitleA quantitative structure-activity relationship study on some sulfolanes and arylthiomethanes acting as HIV-1 protease inhibitors.
[59]
PubMed ID9789740
JournalGen Physiol Biophys
Year1998
Volume17 Suppl 1
Pages3-6
AuthorsLescar J, Stouracova R, Riottot MM, Chitarra V, Brynda J, Fabry M, Horejsi M, Sedlacek J, Bentley GA
TitleStructural studies of HIV-1 protease-inhibiting antibodies.
[60]
CommentsX-ray crystallography
PubMed ID9575185
JournalJ Biol Chem
Year1998
Volume273
Pages12325-31
AuthorsAla PJ, DeLoskey RJ, Huston EE, Jadhav PK, Lam PY, Eyermann CJ, Hodge CN, Schadt MC, Lewandowski FA, Weber PC, McCabe DD, Duke JL, Chang CH
TitleMolecular recognition of cyclic urea HIV-1 protease inhibitors.
Related PDB1hwr
[61]
CommentsX-ray crystallography
PubMed ID9554878
JournalJ Med Chem
Year1998
Volume41
Pages1446-55
AuthorsJadhav PK, Woerner FJ, Lam PY, Hodge CN, Eyermann CJ, Man HW, Daneker WF, Bacheler LT, Rayner MM, Meek JL, Erickson-Viitanen S, Jackson DA, Calabrese JC, Schadt M, Chang CH
TitleNonpeptide cyclic cyanoguanidines as HIV-1 protease inhibitors: synthesis, structure-activity relationships, and X-ray crystal structure studies.
Related PDB1hvh
[62]
CommentsX-ray crystallography
PubMed ID9521105
JournalProtein Sci
Year1998
Volume7
Pages300-5
AuthorsHong L, Hartsuck JA, Foundling S, Ermolieff J, Tang J
TitleActive-site mobility in human immunodeficiency virus, type 1, protease as demonstrated by crystal structure of A28S mutant.
Related PDB1axa
[63]
CommentsX-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 57-155.
Medline ID99043699
PubMed ID9827997
JournalProtein Sci
Year1998
Volume7
Pages2314-23
AuthorsKervinen J, Lubkowski J, Zdanov A, Bhatt D, Dunn BM, Hui KY, Powell DJ, Kay J, Wlodawer A, Gustchina A
TitleToward a universal inhibitor of retroviral proteases: comparative analysis of the interactions of LP-130 complexed with proteases from HIV-1, FIV, and EIAV.
Related PDB1ody
Related UniProtKBP04585
[64]
PubMed ID9672038
JournalProteins
Year1998
Volume32
Pages7-16
AuthorsRick SW, Erickson JW, Burt SK
TitleReaction path and free energy calculations of the transition between alternate conformations of HIV-1 protease.
[65]
CommentsX-ray crystallography
PubMed ID10429209
JournalEur J Biochem
Year1999
Volume263
Pages238-45
AuthorsMahalingam B, Louis JM, Reed CC, Adomat JM, Krouse J, Wang YF, Harrison RW, Weber IT
TitleStructural and kinetic analysis of drug resistant mutants of HIV-1 protease.
Related PDB1dw6,1ebk
[66]
PubMed ID10438521
JournalJ Biol Chem
Year1999
Volume274
Pages23437-42
AuthorsLouis JM, Wondrak EM, Kimmel AR, Wingfield PT, Nashed NT
TitleProteolytic processing of HIV-1 protease precursor, kinetics and mechanism.
[67]
PubMed ID11000004
JournalJ Med Chem
Year2000
Volume43
Pages3495-504
AuthorsTyndall JD, Reid RC, Tyssen DP, Jardine DK, Todd B, Passmore M, March DR, Pattenden LK, Bergman DA, Alewood D, Hu SH, Alewood PF, Birch CJ, Martin JL, Fairlie DP
TitleSynthesis, stability, antiviral activity, and protease-bound structures of substrate-mimicking constrained macrocyclic inhibitors of HIV-1 protease.
[68]
CommentsX-ray crystallography
PubMed ID10651036
JournalProteins
Year2000
Volume38
Pages29-40
AuthorsLi M, Morris GM, Lee T, Laco GS, Wong CH, Olson AJ, Elder JH, Wlodawer A, Gustchina A
TitleStructural studies of FIV and HIV-1 proteases complexed with an efficient inhibitor of FIV protease.
Related PDB3tlh
[69]
PubMed ID10858137
JournalScience
Year2000
Volume288
Pages1590
AuthorsKent S, Marshall GR, Wlodawer A
TitleDetermining the 3D structure of HIV-1 protease.
[70]
PubMed ID11741592
JournalFEBS Lett
Year2001
Volume509
Pages218-24
AuthorsBhavesh NS, Panchal SC, Mittal R, Hosur RV
TitleNMR identification of local structural preferences in HIV-1 protease tethered heterodimer in 6 M guanidine hydrochloride.
[71]
CommentsX-ray crystallography
PubMed ID11170625
JournalJ Med Chem
Year2001
Volume44
Pages155-69
AuthorsSchaal W, Karlsson A, Ahlsen G, Lindberg J, Andersson HO, Danielson UH, Classon B, Unge T, Samuelsson B, Hulten J, Hallberg A, Karlen A
TitleSynthesis and comparative molecular field analysis (CoMFA) of symmetric and nonsymmetric cyclic sulfamide HIV-1 protease inhibitors.
Related PDB1g2k
[72]
PubMed ID11410934
JournalMed Res Rev
Year2001
Volume21
Pages348-53
AuthorsMager PP
TitleThe active site of HIV-1 protease.
[73]
CommentsX-ray crystallography
PubMed ID11340661
JournalProteins
Year2001
Volume43
Pages455-64
AuthorsMahalingam B, Louis JM, Hung J, Harrison RW, Weber IT
TitleStructural implications of drug-resistant mutants of HIV-1 protease: high-resolution crystal structures of the mutant protease/substrate analogue complexes.
Related PDB1fej,1ff0,1fff,1ffi,1fg6,1fg8,1fgc
[74]
CommentsX-ray crystallography
PubMed ID11170214
JournalProteins
Year2001
Volume43
Pages57-64
AuthorsPillai B, Kannan KK, Hosur MV
Title1.9 A x-ray study shows closed flap conformation in crystals of tethered HIV-1 PR.
Related PDB1g6l
[75]
PubMed ID11591344
JournalStructure
Year2001
Volume9
Pages887-95
AuthorsRezacova P, Lescar J, Brynda J, Fabry M, Horejsi M, Sedlacek J, Bentley GA
TitleStructural basis of HIV-1 and HIV-2 protease inhibition by a monoclonal antibody.
[76]
CommentsX-ray crystallography
PubMed ID12051725
JournalBiochem Biophys Res Commun
Year2002
Volume294
Pages395-401
AuthorsKumar M, Kannan KK, Hosur MV, Bhavesh NS, Chatterjee A, Mittal R, Hosur RV
TitleEffects of remote mutation on the autolysis of HIV-1 PR: X-ray and NMR investigations.
Related PDB1lv1
[77]
PubMed ID12034371
JournalBiochem Pharmacol
Year2002
Volume63
Pages1863-73
AuthorsLebon F, Boggetto N, Ledecq M, Durant F, Benatallah Z, Sicsic S, Lapouyade R, Kahn O, Mouithys-Mickalad A, Deby-Dupont G, Reboud-Ravaux M. Metal-organic compounds: a new approach for drug discovery
TitleN1-(4-methyl-2-pyridyl)-2,3,6-trimethoxybenzamide copper(II) complex as an inhibitor of human immunodeficiency virus 1 protease.
[78]
PubMed ID11802730
JournalBiochemistry
Year2002
Volume41
Pages1302-7
AuthorsPorter DJ, Hanlon MH, Furfine ES
TitleHIV-1 protease: characterization of a catalytically competent enzyme-substrate intermediate.
[79]
PubMed ID12124265
JournalBiophys J
Year2002
Volume83
Pages794-807
AuthorsTrylska J, Bala P, Geller M, Grochowski P
TitleMolecular dynamics simulations of the first steps of the reaction catalyzed by HIV-1 protease.
[80]
PubMed ID11906284
JournalJ Med Chem
Year2002
Volume45
Pages1432-8
AuthorsDohnalek J, Hasek J, Duskova J, Petrokova H, Hradilek M, Soucek M, Konvalinka J, Brynda J, Sedlacek J, Fabry M
TitleHydroxyethylamine isostere of an HIV-1 protease inhibitor prefers its amine to the hydroxy group in binding to catalytic aspartates. A synchrotron study of HIV-1 protease in complex with a peptidomimetic inhibitor.
[81]
PubMed ID12051929
JournalJ Mol Biol
Year2002
Volume319
Pages567-83
AuthorsPiana S, Carloni P, Parrinello M
TitleRole of conformational fluctuations in the enzymatic reaction of HIV-1 protease.
[82]
PubMed ID11771964
JournalJ Mol Biol
Year2002
Volume315
Pages21-52
AuthorsZoete V, Michielin O, Karplus M
TitleRelation between sequence and structure of HIV-1 protease inhibitor complexes: a model system for the analysis of protein flexibility.
[83]
PubMed ID11773409
JournalJ Virol
Year2002
Volume76
Pages1349-58
AuthorsYoshimura K, Kato R, Kavlick MF, Nguyen A, Maroun V, Maeda K, Hussain KA, Ghosh AK, Gulnik SV, Erickson JW, Mitsuya H
TitleA potent human immunodeficiency virus type 1 protease inhibitor, UIC-94003 (TMC-126), and selection of a novel (A28S) mutation in the protease active site.
[84]
CommentsX-ray crystallography
PubMed ID11790852
JournalProtein Sci
Year2002
Volume11
Pages418-29
AuthorsKing NM, Melnick L, Prabu-Jeyabalan M, Nalivaika EA, Yang SS, Gao Y, Nie X, Zepp C, Heefner DL, Schiffer CA
TitleLack of synergy for inhibitors targeting a multi-drug-resistant HIV-1 protease.
Related PDB1k6c,1k6p,1k6t,1k6v
[85]
PubMed ID12237461
JournalProtein Sci
Year2002
Volume11
Pages2393-402
AuthorsPiana S, Carloni P, Rothlisberger U
TitleDrug resistance in HIV-1 protease: Flexibility-assisted mechanism of compensatory mutations.
[86]
CommentsX-ray crystallography
PubMed ID12012342
JournalProteins
Year2002
Volume48
Pages107-16
AuthorsMahalingam B, Boross P, Wang YF, Louis JM, Fischer CC, Tozser J, Harrison RW, Weber IT
TitleCombining mutations in HIV-1 protease to understand mechanisms of resistance.
Related PDB1k1t,1k1u,1k2b,1k2c
[87]
PubMed ID12005435
JournalStructure
Year2002
Volume10
Pages369-81
AuthorsPrabu-Jeyabalan M, Nalivaika E, Schiffer CA
TitleSubstrate shape determines specificity of recognition for HIV-1 protease: analysis of crystal structures of six substrate complexes.
[88]
PubMed ID12534275
JournalBiochemistry
Year2003
Volume42
Pages631-8
AuthorsMuzammil S, Ross P, Freire E
TitleA major role for a set of non-active site mutations in the development of HIV-1 protease drug resistance.
[89]
PubMed ID12564936
JournalBiochemistry
Year2003
Volume42
Pages1326-33
AuthorsZhu Z, Schuster DI, Tuckerman ME
TitleMolecular dynamics study of the connection between flap closing and binding of fullerene-based inhibitors of the HIV-1 protease.
[90]
PubMed ID12675950
JournalBMC Struct Biol
Year2003
Volume3
Pages2
AuthorsJenwitheesuk E, Samudrala R
TitleImproved prediction of HIV-1 protease-inhibitor binding energies by molecular dynamics simulations.
[91]
PubMed ID12644464
JournalJ Biol Chem
Year2003
Volume278
Pages19980-5
AuthorsBhavesh NS, Sinha R, Mohan PM, Hosur RV
TitleNMR elucidation of early folding hierarchy in HIV-1 protease.
[92]
PubMed ID12933791
JournalJ Biol Chem
Year2003
Volume278
Pages43311-9
AuthorsIshima R, Torchia DA, Lynch SM, Gronenborn AM, Louis JM
TitleSolution structure of the mature HIV-1 protease monomer: insight into the tertiary fold and stability of a precursor.
[93]
PubMed ID12696052
JournalProteins
Year2003
Volume51
Pages409-22
AuthorsKurt N, Scott WR, Schiffer CA, Haliloglu T
TitleCooperative fluctuations of unliganded and substrate-bound HIV-1 protease: a structure-based analysis on a variety of conformations from crystallography and molecular dynamics simulations.
[94]
PubMed ID15317462
JournalJ Med Chem
Year2004
Volume47
Pages4507-16
AuthorsFornabaio M, Spyrakis F, Mozzarelli A, Cozzini P, Abraham DJ, Kellogg GE
TitleSimple, intuitive calculations of free energy of binding for protein-ligand complexes. 3. The free energy contribution of structural water molecules in HIV-1 protease complexes.
[95]
PubMed ID15184023
JournalJ Mol Biol
Year2004
Volume340
Pages67-79
AuthorsLevy Y, Caflisch A, Onuchic JN, Wolynes PG
TitleThe folding and dimerization of HIV-1 protease: evidence for a stable monomer from simulations.
[96]
PubMed ID15066436
JournalJ Mol Biol
Year2004
Volume338
Pages341-52
AuthorsTie Y, Boross PI, Wang YF, Gaddis L, Hussain AK, Leshchenko S, Ghosh AK, Louis JM, Harrison RW, Weber IT
TitleHigh resolution crystal structures of HIV-1 protease with a potent non-peptide inhibitor (UIC-94017) active against multi-drug-resistant clinical strains.
[97]
PubMed ID14990731
JournalJ Virol
Year2004
Volume78
Pages3123-32
AuthorsLogsdon BC, Vickrey JF, Martin P, Proteasa G, Koepke JI, Terlecky SR, Wawrzak Z, Winters MA, Merigan TC, Kovari LC
TitleCrystal structures of a multidrug-resistant human immunodeficiency virus type 1 protease reveal an expanded active-site cavity.
[98]
PubMed ID15289598
JournalProc Natl Acad Sci U S A
Year2004
Volume101
Pages11640-5
AuthorsFernandez A, Rogale K, Scott R, Scheraga HA
TitleInhibitor design by wrapping packing defects in HIV-1 proteins.
[99]
PubMed ID15044738
JournalProtein Sci
Year2004
Volume13
Pages1108-23
AuthorsPerryman AL, Lin JH, McCammon JA
TitleHIV-1 protease molecular dynamics of a wild-type and of the V82F/I84V mutant: possible contributions to drug resistance and a potential new target site for drugs.
[100]
PubMed ID14739332
JournalProtein Sci
Year2004
Volume13
Pages513-28
AuthorsTrylska J, Grochowski P, McCammon JA
TitleThe role of hydrogen bonding in the enzymatic reaction catalyzed by HIV-1 protease.

comments
The protein, POL polyprotein from HIV-1, is composed of the following enzymes, protease (E.C. 3.4.23.16), reverse transcriptase (E.C. 2.7.7.49), ribonuclease H (E.C. 3.1.26.4) and integrase.
This entry corresponds to the protease domain, which belongs to the peptidase family-A2.
According to the literature, this enzyme has got a similar catalytic mechanism to that of pepsin (D00436 in EzCatDB).

createdupdated
2004-03-052012-07-03


Copyright: Nozomi Nagano, JST & CBRC-AIST
Funded by PRESTO/Japan Science and Technology Corporation (JST) (December 2001 - November 2004)
Funded by Grant-in-Aid for Publication of Scientific Research Results/Japan Society for the Promotion of Science (JSPS) (April 2005 - March 2006)
Funded by Grant-in-Aid for Scientific Research (B)/Japan Society for the Promotion of Science (JSPS) (April 2005 - March 2008)
Funded by BIRD/Japan Science and Technology Corporation (JST) (September 2005 - September 2008)
Funded by BIRD/Japan Science and Technology Corporation (JST) (October 2007 - September 2010)
Funded by Grant-in-Aid for Publication of Scientific Research Results/Japan Society for the Promotion of Science (JSPS) (April 2011 - March 2012)
Funded by Grant-in-Aid for Publication of Scientific Research Results/Japan Society for the Promotion of Science (JSPS) (April 2012 - March 2013)
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