EzCatDB: M00181
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DB codeM00181
RLCP classification1.13.30000.10 : Hydrolysis
CATH domainDomain 12.40.10.10 : Thrombin, subunit HCatalytic domain
Domain 22.40.10.10 : Thrombin, subunit HCatalytic domain
Domain 32.40.10.10 : Thrombin, subunit H
Domain 42.40.10.10 : Thrombin, subunit H
Domain 52.10.90.10 : Cystine Knot Cytokines, subunit B
E.C.3.4.21.35

CATH domainRelated DB codes (homologues)
2.40.10.10 : Thrombin, subunit HM00139,D00214,M00167,D00426,M00133,D00428,D00429,D00430,D00431,D00432,D00433,D00434,D00435,M00227,M00209,D00194,D00197,D00211,D00212,D00216,M00212,D00224,D00497,M00217,M00216,D00528,D00848,D00850,D00851,D00852,D00855,M00152,M00155,M00157,M00315,M00316,M00317,M00348,M00349,T00074,T00410,T00411

Enzyme Name
UniProtKBKEGG

P00756P00757P01139
Protein nameKallikrein 1-related peptidase b3Kallikrein 1-related peptidase-like b4Beta-nerve growth factortissue kallikrein
glandular kallikrein
pancreatic kallikrein
submandibular kallikrein
submaxillary kallikrein
kidney kallikrein
urinary kallikrein
kallikrein
salivary kallikrein
kininogenin
kininogenase
callicrein
glumorin
padreatin
padutin
kallidinogenase
bradykininogenase
depot-padutin
urokallikrein
dilminal D
onokrein P
SynonymsEC 3.4.21.35
Glandular kallikrein K3
mGK-3
Tissue kallikrein-3
7S nerve growth factor gamma chain
Gamma-NGF
7S nerve growth factor alpha chain
Alpha-NGF
Beta-NGF
ContainsNerve growth factor gamma chain 1
Nerve growth factor gamma chain 2
NoneNone
RefSeqNP_032719.1 (Protein)
NM_008693.2 (DNA/RNA sequence)
NP_035045.2 (Protein)
NM_010915.3 (DNA/RNA sequence)
NP_001106168.1 (Protein)
NM_001112698.1 (DNA/RNA sequence)
NP_038637.1 (Protein)
NM_013609.2 (DNA/RNA sequence)
MEROPSS01.170 (Serine)
S01.931 (Serine)

PfamPF00089 (Trypsin)
[Graphical view]
PF00089 (Trypsin)
[Graphical view]
PF00243 (NGF)
[Graphical view]


UniProtKB:Accession NumberP00756P00757P01139
Entry nameK1KB3_MOUSEK1KB4_MOUSENGF_MOUSE
ActivityPreferential cleavage of Arg-|-Xaa bonds in small molecule substrates. Highly selective action to release kallidin (lysyl-bradykinin) from kininogen involves hydrolysis of Met-|-Xaa or Leu-|-Xaa.

Subunit7S nerve growth factor is composed of two alpha chains, a beta dimer composed of identical chains, and two gamma chains.7S nerve growth factor is composed of two alpha chains, a beta dimer composed of identical chains, and two gamma chains.Homodimer.
Subcellular location

Secreted.
CofactorBinds 2 zinc ions per 7S complex. The zinc ions are bound at the alpha-gamma interfaces.Binds 2 zinc ions per 7S complex. The zinc ions are bound at the alpha-gamma interfaces.

Compound table: links to PDB-related databases & PoSSuM

CofactorsSubstratesProductsintermediates
KEGG-idC00038C00017C00012C00769C00001C00012C01505C00306I00087I00085I00086
CompoundZincProteinPeptideKininogenH2OPeptideKallidinBradykininPeptidyl-tetrahedral intermediateAcyl-enzymeTetrahedral intermediate
Typeheavy metalpeptide/proteinpeptide/proteinpeptide/proteinH2Opeptide/proteinamino acids,amine group,aromatic ring (only carbon atom),carbohydrate,carboxyl group,imine group,lipid,peptide/proteinamino acids,amine group,aromatic ring (only carbon atom),carbohydrate,carboxyl group,imine group,lipid,peptide/protein


ChEBI29105



15377

6102
3165



PubChem32051



962
22247451

5311111
439201



                   
1sgfG01Bound:_ZNUnboundUnboundUnbound UnboundUnboundUnbound   
1sgfZ01Bound:_ZNUnboundUnboundUnbound UnboundUnboundUnbound   
1sgfG02UnboundUnboundUnboundUnbound UnboundUnboundUnbound   
1sgfZ02UnboundUnboundUnboundUnbound UnboundUnboundUnbound   
1sgfA01UnboundUnboundUnboundUnbound UnboundUnboundUnbound   
1sgfX01UnboundUnboundUnboundUnbound UnboundUnboundUnbound   
1sgfA02UnboundUnboundUnboundUnbound UnboundUnboundUnbound   
1sgfX02UnboundUnboundUnboundUnbound UnboundUnboundUnbound   
1sgfBUnboundUnboundUnboundUnbound UnboundUnboundUnbound   
1sgfYUnboundUnboundUnboundUnbound UnboundUnboundUnbound   

Active-site residues
pdbCatalytic residuesCofactor-binding residuesMain-chain involved in catalysiscomment
            
1sgfG01SER 195
HIS 217;GLU 222(Zinc binding)
GLY 193;SER 195
 
1sgfZ01SER 195
HIS 217;GLU 222(Zinc binding)
GLY 193;SER 195
 
1sgfG02HIS 57;ASP 102
 
 
 
1sgfZ02HIS 57;ASP 102
 
 
 
1sgfA01 
 
 
 
1sgfX01 
 
 
 
1sgfA02 
GLU 75;HIS 82(Zinc binding)
 
 
1sgfX02 
      ;HIS 82(Zinc binding)
 
invisible 71-76, 78-79
1sgfB 
 
 
 
1sgfY 
 
 
 


references
[1]
PubMed ID8401208
JournalProtein Sci
Year1993
Volume2
Pages1229-41
AuthorsBax B, Blaber M, Ferguson G, Sternberg MJ, Walls PH
TitlePrediction of the three-dimensional structures of the nerve growth factor and epidermal growth factor binding proteins (kallikreins) and an hypothetical structure of the high molecular weight complex of epidermal growth factor with its binding protein.
[2]
CommentsX-RAY CRYSTALLOGRAPHY (3.15 ANGSTROMS) OF 7S COMPLEX.
PubMed ID9351801
JournalStructure
Year1997
Volume5
Pages1275-85
AuthorsBax B, Blundell TL, Murray-Rust J, McDonald NQ
TitleStructure of mouse 7S NGF: a complex of nerve growth factor with four binding proteins.
Related PDB1sgf
Related UniProtKBP00756

comments
This enzyme belongs to the peptidase family-S1.
This enzyme, 7S nerve growth factor, is composed of two alpha chains, a beta dimer composed of identical chains, and two gamma chains. The alpha and gamma chains belong to the peptidase family-S1. However, although the gamma chains have got peptidase activity, the alpha chains do not have activity.
Although this enzyme binds two zinc ions per complex, they are not involved in catalysis, as they bound at the interface of alpha/gamma subunits.
The gamma subunits have got a catalytic triad, composed of Ser/His/Asp and an oxyanionhole of mainchain amide groups. Thus, it must have a similar reaction mechanism to that of trypsin (D00197 in EzCatDB).

createdupdated
2006-01-102011-02-18


Copyright: Nozomi Nagano, JST & CBRC-AIST
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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)
Supported by the commission for the Development of Artificial Gene Synthesis Technology for Creating Innovative Biomaterial from the Ministry of Economy, Trade and Industry (METI) (October 2012 - )
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