DB code: M00206

RLCP classification 1.13.200.966 : Hydrolysis
CATH domain -.-.-.- :
2.40.70.10 : Cathepsin D, subunit A; domain 1 Catalytic domain
3.10.10.10 : HIV Type 1 Reverse Transcriptase; Chain A, domain 1
3.30.70.270 : Alpha-Beta Plaits
3.30.70.270 : Alpha-Beta Plaits
3.30.70.270 : Alpha-Beta Plaits
3.30.420.10 : Nucleotidyltransferase; domain 5
2.70.40.10 : Deoxyuridine 5'-Triphosphate Nucleotidohydrolase; Chain A Catalytic domain
1.10.10.200 : Arc Repressor Mutant, subunit A
3.30.420.10 : Nucleotidyltransferase; domain 5
2.30.30.10 : SH3 type barrels.
E.C. 3.4.23.- 2.7.7.49 3.1.26.4 3.6.1.23
CSA
M-CSA
MACiE

CATH domain Related DB codes (homologues)
1.10.10.200 : Arc Repressor Mutant, subunit A M00166
2.30.30.10 : SH3 type barrels. M00135 M00146
2.40.70.10 : Cathepsin D, subunit A; domain 1 D00471 D00436 D00438 D00439 D00440 D00441 D00442 D00443 D00437 D00444 D00423 D00445 D00484 M00166 D00231 D00529
2.70.40.10 : Deoxyuridine 5'-Triphosphate Nucleotidohydrolase; Chain A T00231
3.10.10.10 : HIV Type 1 Reverse Transcriptase; Chain A, domain 1 M00135 M00146 M00166
3.30.420.10 : Nucleotidyltransferase; domain 5 T00252 M00019 M00020 M00055 M00135 M00146 M00166 M00173 M00175 M00186
3.30.70.270 : Alpha-Beta Plaits M00019 M00135 M00146 M00166 M00209

Uniprot Enzyme Name
UniprotKB Protein name Synonyms Contains Pfam
P16088 Pol polyprotein
None Protease Retropepsin
EC 3.4.23.-
Reverse transcriptase/ribonuclease H
(RT)
EC 2.7.7.49
EC 3.1.26.4
Deoxyuridine 5''-triphosphate nucleotidohydrolase
(dUTPase)
EC 3.6.1.23
Integrase
(IN)
PF00692 (dUTPase)
PF00552 (IN_DBD_C)
PF02022 (Integrase_Zn)
PF00075 (RNase_H)
PF00665 (rve)
PF00077 (RVP)
PF00078 (RVT_1)
PF06815 (RVT_connect)
PF06817 (RVT_thumb)
[Graphical View]

KEGG enzyme name
RNA-directed DNA polymerase
(EC 2.7.7.49 )
DNA nucleotidyltransferase (RNA-directed)
(EC 2.7.7.49 )
reverse transcriptase
(EC 2.7.7.49 )
revertase
(EC 2.7.7.49 )
RNA-dependent deoxyribonucleate nucleotidyltransferase
(EC 2.7.7.49 )
RNA revertase
(EC 2.7.7.49 )
RNA-dependent DNA polymerase
(EC 2.7.7.49 )
RNA-instructed DNA polymerase
(EC 2.7.7.49 )
RT
(EC 2.7.7.49 )
calf thymus ribonuclease H
(EC 3.1.26.4 )
endoribonuclease H (calf thymus)
(EC 3.1.26.4 )
RNase H
(EC 3.1.26.4 )
RNA*DNA hybrid ribonucleotidohydrolase
(EC 3.1.26.4 )
hybrid ribonuclease
(EC 3.1.26.4 )
hybridase
(EC 3.1.26.4 )
hybridase (ribonuclease H)
(EC 3.1.26.4 )
ribonuclease H
(EC 3.1.26.4 )
hybrid nuclease
(EC 3.1.26.4 )
dUTP diphosphatase
(EC 3.6.1.23 )
deoxyuridine-triphosphatase
(EC 3.6.1.23 )
dUTPase
(EC 3.6.1.23 )
dUTP pyrophosphatase
(EC 3.6.1.23 )
desoxyuridine 5'-triphosphate nucleotidohydrolase
(EC 3.6.1.23 )
desoxyuridine 5'-triphosphatase
(EC 3.6.1.23 )

UniprotKB: Accession Number Entry name Activity Subunit Subcellular location Cofactor
P16088 POL_FIVPE Endonucleolytic cleavage to 5''- phosphomonoester. dUTP + H(2)O = dUMP + diphosphate. Deoxynucleoside triphosphate + DNA(n) = diphosphate + DNA(n+1).

KEGG Pathways
Map code Pathways E.C.
MAP00240 Pyrimidine metabolism 3.6.1.23

Compound table
Cofactors Substrates Products Intermediates
KEGG-id C00305 C00017 C00012 C00677 C00039 C00046 C00460 C00001 C00017 C00012 C00039 C00960 C00365 C00013 I00136
E.C. 3.4.23.-
3.4.23.-
2.7.7.49
2.7.7.49
3.1.26.4
3.6.1.23
3.4.23.-
3.1.26.4
3.6.1.23
3.4.23.-
3.4.23.-
2.7.7.49
3.1.26.4
3.6.1.23
2.7.7.49
3.6.1.23
3.4.23.-
Compound Magnesium Protein Peptide Deoxynucleoside triphosphate DNA(n) RNA dUTP H2O Protein Peptide DNA(n+1) RNA 5'-phosphate dUMP Pyrophosphate Amino-diol-tetrahedral intermediate
Type divalent metal (Ca2+, Mg2+) peptide/protein peptide/protein nucleotide nucleic acids nucleic acids amide group,nucleotide H2O peptide/protein peptide/protein nucleic acids nucleic acids,phosphate group/phosphate ion amide group,nucleotide phosphate group/phosphate ion
ChEBI 18420
17625
15377
17622
29888
PubChem 888
65070
962
22247451
65063
21961011
1023
1b11A Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Analogue:INT Unbound Unbound Unbound Unbound Unbound
1fivA Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Transition-state-analogue:ACE-ALN-VAL-STA-GLU-ALN
2fivA Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Transition-state-analogue:ACE-ALN-VAL-STA-GLU-ALN-NH2
3fivA Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Analogue:ACE-ALN-VAL-LEU-ALA-GLU-ALN-NH2 (chain I, J) Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound
4fivA Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Transition-state-analogue:LP1
5fivA Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Analogue:INT Unbound Unbound Unbound Unbound Unbound
6fivA Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Analogue:INT Unbound Unbound Unbound Unbound Unbound
2fivB Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound
3fivB Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound
1dutA Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Bound:_MG Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound
1dutB Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Bound:_MG Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound
1f7dA Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Bound:_MG Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound
1f7dB Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Bound:_MG Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound
1f7kA Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Bound:_MG Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Bound:UMP Unbound Unbound
1f7kB Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Bound:_MG Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Bound:UMP Unbound Unbound
1f7nA Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Bound:_MG Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Bound:UMP Unbound Unbound
1f7nB Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Bound:_MG Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Bound:UMP Unbound Unbound
1f7oA Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound
1f7oB Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound
1f7oC Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound
1f7pA Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound Unbound Unbound Unbound Analogue:UDP Unbound Unbound Unbound Unbound Unbound Unbound Unbound
1f7pB Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound
1f7pC Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound Unbound Unbound Unbound Analogue:UDP Unbound Unbound Unbound Unbound Unbound Unbound Unbound
1f7qA Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound Unbound Unbound Unbound Bound:DUT Bound:HOH_658 Unbound Unbound Unbound Unbound Unbound Unbound Unbound
1f7qB Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound
1f7qC Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound Unbound Unbound Unbound Bound:DUT Bound:HOH_646 Unbound Unbound Unbound Unbound Unbound Unbound Unbound
1f7rA Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Bound:_MG Unbound Unbound Unbound Unbound Unbound Analogue:UDP Unbound Unbound Unbound Unbound Unbound Unbound Unbound

Reference for Active-site residues
resource references E.C.
Swiss-prot;P16088

Active-site residues
PDB Catalytic residues Cofactor-binding residues Modified residues Main-chain involved in catalysis Comment
1b11A Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain ASP 30 (EC 3.4.23.-)
1fivA Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain ASP 30 (EC 3.4.23.-)
2fivA Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain (EC 3.4.23.-) mutant D30N
3fivA Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain (EC 3.4.23.-) mutant D30N
4fivA Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain ASP 30 (EC 3.4.23.-)
5fivA Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain ASP 30 (EC 3.4.23.-)
6fivA Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain ASP 30 (EC 3.4.23.-)
2fivB Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain (EC 3.4.23.-) mutant D30N
3fivB Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain (EC 3.4.23.-) mutant D30N
1dutA Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain LYS 55;ASP 71;LYS 97;GLN 100 ASP 64(magnesium binding) SER 56;SER 57 (EC 3.6.1.23)
1dutB Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain LYS 55;ASP 71;LYS 97;GLN 100 ASP 64(magnesium binding) SER 56;SER 57 (EC 3.6.1.23)
1f7dA Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain LYS 55;ASP 71;LYS 97;GLN 100 ASP 64(magnesium binding) SER 56;SER 57 (EC 3.6.1.23)
1f7dB Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain LYS 255;ASP 271;LYS 297;GLN 300 ASP 264(magnesium binding) SER 256;SER 257 (EC 3.6.1.23)
1f7kA Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain LYS 55;ASP 71;LYS 97;GLN 100 ASP 64(magnesium binding) SER 56;SER 57 (EC 3.6.1.23)
1f7kB Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain LYS 255;ASP 271;LYS 297;GLN 300 ASP 264(magnesium binding) SER 256;SER 257 (EC 3.6.1.23)
1f7nA Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain LYS 55;ASP 71;LYS 97;GLN 100 ASP 64(magnesium binding) SER 56;SER 57 (EC 3.6.1.23)
1f7nB Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain LYS 255;ASP 271;LYS 297;GLN 300 ASP 264(magnesium binding) SER 256;SER 257 (EC 3.6.1.23)
1f7oA Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain LYS 55;ASP 71;LYS 97;GLN 100 ASP 64(magnesium binding) SER 56;SER 57 (EC 3.6.1.23)
1f7oB Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain LYS 255;ASP 271;LYS 297;GLN 300 ASP 264(magnesium binding) SER 256;SER 257 (EC 3.6.1.23)
1f7oC Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain LYS 455;ASP 471;LYS 497;GLN 500 ASP 464(magnesium binding) SER 456;SER 457 (EC 3.6.1.23)
1f7pA Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain LYS 55;ASP 71;LYS 97;GLN 100 ASP 64(magnesium binding) SER 56;SER 57 (EC 3.6.1.23)
1f7pB Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain LYS 255;ASP 271;LYS 297;GLN 300 ASP 264(magnesium binding) SER 256;SER 257 (EC 3.6.1.23)
1f7pC Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain LYS 455;ASP 471;LYS 497;GLN 500 ASP 464(magnesium binding) SER 456;SER 457 (EC 3.6.1.23)
1f7qA Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain LYS 55;ASP 71;LYS 97;GLN 100 ASP 64(magnesium binding) SER 56;SER 57 (EC 3.6.1.23)
1f7qB Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain LYS 255;ASP 271;LYS 297;GLN 300 ASP 264(magnesium binding) SER 256;SER 257 (EC 3.6.1.23)
1f7qC Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain LYS 455;ASP 471;LYS 497;GLN 500 ASP 464(magnesium binding) SER 456;SER 457 (EC 3.6.1.23)
1f7rA Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain LYS 55;ASP 71;LYS 97;GLN 100 ASP 64(magnesium binding) SER 56;SER 57 (EC 3.6.1.23)

References for Catalytic Mechanism
References Sections No. of steps in catalysis
[2]
Fig.1
[4]
Fig.8, p.10705-10707

References
[1]
Resource
Comments X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 42-154. Retropepsin (3.4.23.-)
Medline ID 95393228
PubMed ID 7664111
Journal Nat Struct Biol
Year 1995
Volume 2
Pages 480-8
Authors Wlodawer A, Gustchina A, Reshetnikova L, Lubkowski J, Zdanov A, Hui KY, Angleton EL, Farmerie WG, Goodenow MM, Bhatt D, et al
Title Structure of an inhibitor complex of the proteinase from feline immunodeficiency virus.
Related PDB 1fiv
Related UniProtKB P16088
[2]
Resource
Comments Retropepsin (3.4.23.-)
Medline ID
PubMed ID 9022971
Journal Bioorg Med Chem
Year 1996
Volume 4
Pages 2055-69
Authors Qian X, Moris-Varas F, Fitzgerald MC, Wong CH
Title C2-symmetrical tetrahydroxyazepanes as inhibitors of glycosidases and HIV/FIV proteases.
Related PDB
Related UniProtKB
[3]
Resource
Comments dUTP pyrophosphatase (3.6.1.23)
Medline ID
PubMed ID 8976551
Journal Protein Sci
Year 1996
Volume 5
Pages 2429-37
Authors Prasad GS, Stura EA, McRee DE, Laco GS, Hasselkus-Light C, Elder JH, Stout CD
Title Crystal structure of dUTP pyrophosphatase from feline immunodeficiency virus.
Related PDB 1dut
Related UniProtKB
[4]
Resource
Comments X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 42-154. Retropepsin (3.4.23.-)
Medline ID 97419133
PubMed ID 9271500
Journal Biochemistry
Year 1997
Volume 36
Pages 10696-708
Authors Laco GS, Schalk-Hihi C, Lubkowski J, Morris G, Zdanov A, Olson A, Elder JH, Wlodawer A, Gustchina A
Title Crystal structures of the inactive D30N mutant of feline immunodeficiency virus protease complexed with a substrate and an inhibitor.
Related PDB 2fiv 3fiv
Related UniProtKB P16088
[5]
Resource
Comments X-ray crystallography. Retropepsin (3.4.23.-)
Medline ID
PubMed ID 9827997
Journal Protein Sci
Year 1998
Volume 7
Pages 2314-23
Authors Kervinen J, Lubkowski J, Zdanov A, Bhatt D, Dunn BM, Hui KY, Powell DJ, Kay J, Wlodawer A, Gustchina A
Title Toward a universal inhibitor of retroviral proteases: comparative analysis of the interactions of LP-130 complexed with proteases from HIV-1, FIV, and EIAV.
Related PDB 4fiv
Related UniProtKB
[6]
Resource
Comments Retropepsin (3.4.23.-)
Medline ID
PubMed ID 10380354
Journal Biopolymers
Year 1999
Volume 51
Pages 69-77
Authors Dunn BM, Pennington MW, Frase DC, Nash K
Title Comparison of inhibitor binding to feline and human immunodeficiency virus proteases: structure-based drug design and the resistance problem.
Related PDB
Related UniProtKB
[7]
Resource
Comments Retropepsin (3.4.23.-)
Medline ID
PubMed ID 10409825
Journal Proteins
Year 1999
Volume 36
Pages 318-31
Authors Dominy BN, Brooks CL 3rd
Title Methodology for protein-ligand binding studies: application to a model for drug resistance, the HIV/FIV protease system.
Related PDB
Related UniProtKB
[8]
Resource
Comments dUTP pyrophosphatase (3.6.1.23)
Medline ID
PubMed ID 10329142
Journal J Mol Biol
Year 1999
Volume 288
Pages 275-87
Authors Harris JM, McIntosh EM, Muscat GE
Title Structure/function analysis of a dUTPase: catalytic mechanism of a potential chemotherapeutic target.
Related PDB
Related UniProtKB
[9]
Resource
Comments X-ray crystallography. Retropepsin (3.4.23.-)
Medline ID
PubMed ID 10651036
Journal Proteins
Year 2000
Volume 38
Pages 29-40
Authors Li M, Morris GM, Lee T, Laco GS, Wong CH, Olson AJ, Elder JH, Wlodawer A, Gustchina A
Title Structural studies of FIV and HIV-1 proteases complexed with an efficient inhibitor of FIV protease.
Related PDB 1b11 5fiv 6fiv
Related UniProtKB
[10]
Resource
Comments dUTP pyrophosphatase (3.6.1.23)
Medline ID
PubMed ID 10957629
Journal Acta Crystallogr D Biol Crystallogr
Year 2000
Volume 56
Pages 1100-9
Authors Prasad GS, Stura EA, Elder JH, Stout CD
Title Structures of feline immunodeficiency virus dUTP pyrophosphatase and its nucleotide complexes in three crystal forms.
Related PDB 1f7d 1f7k 1f7n 1f7o 1f7p 1f7q 1f7r
Related UniProtKB
[11]
Resource
Comments Retropepsin (3.4.23.-)
Medline ID
PubMed ID 11206463
Journal Bioorg Med Chem Lett
Year 2001
Volume 11
Pages 219-22
Authors Mak CC, Le VD, Lin YC, Elder JH, Wong CH
Title Design, synthesis, and biological evaluation of HIV/FIV protease inhibitors incorporating a conformationally constrained macrocycle with a small P3' residue.
Related PDB
Related UniProtKB
[12]
Resource
Comments Retropepsin (3.4.23.-)
Medline ID
PubMed ID 12767979
Journal J Virol
Year 2003
Volume 77
Pages 6589-600
Authors Lin YC, Beck Z, Morris GM, Olson AJ, Elder JH
Title Structural basis for distinctions between substrate and inhibitor specificities for feline immunodeficiency virus and human immunodeficiency virus proteases.
Related PDB
Related UniProtKB
[13]
Resource
Comments Retropepsin (3.4.23.-)
Medline ID
PubMed ID 15289598
Journal Proc Natl Acad Sci U S A
Year 2004
Volume 101
Pages 11640-5
Authors Fernandez A, Rogale K, Scott R, Scheraga HA
Title Inhibitor design by wrapping packing defects in HIV-1 proteins.
Related PDB
Related UniProtKB
[14]
Resource
Comments dUTP pyrophosphatase (3.6.1.23)
Medline ID
PubMed ID 16154087
Journal Structure
Year 2005
Volume 13
Pages 1299-310
Authors Tarbouriech N, Buisson M, Seigneurin JM, Cusack S, Burmeister WP
Title The monomeric dUTPase from Epstein-Barr virus mimics trimeric dUTPases.
Related PDB
Related UniProtKB

Comments
This enzyme is composed of retropepsin (EC 3.4.23.-), RNA-directed DNA polymerase (EC 2.7.7.49), RNase H (EC 3.1.26.4), dUTP pyrophosphatase (EC 3.6.1.23), and integrase.
The tertiary structures have been solved only for retropepsin (EC 3.4.23.-) and dUTP pyrophosphatase (EC 3.6.1.23). The dUTP pyrophosphatase domain (EC 3.6.1.23) forms a trimer, which binds one Mg2+ ion (see PDB;1dut).
The domains which corresponds to protease domain (EC 3.4.23.-) belong to the peptidase family-A2.
Although this domain has a catalytic aspartic residue, it forms a homodimer with a single active site with a typical catalytic dyad, composed of two aspartic acid residues. According to the literature [4], the catalytic mechanism is very similar to that of pepsin (see D00436 in EzCatDB).

Created Updated
2004-03-19 2012-06-28