EzCatDB: S00398
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DB codeS00398
RLCP classification1.13.11400.460 : Hydrolysis
CATH domainDomain 13.40.390.10 : Collagenase (Catalytic Domain)Catalytic domain
E.C.3.4.24.42

CATH domainRelated DB codes (homologues)
3.40.390.10 : Collagenase (Catalytic Domain)S00394,S00395,S00397,S00399,D00232,D00236,M00101

Enzyme Name
UniProtKBKEGG

P15167
Protein nameZinc metalloproteinase atrolysin-Datrolysin C
Crotalus atrox metalloendopeptidase c
hemorrhagic toxin c and d
SynonymsEC 3.4.24.42
Hemorrhagic metalloproteinase atrolysin D
Hemorrhagic toxin D
HT-D
MEROPSM12.144 (Metallo)
PfamPF01562 (Pep_M12B_propep)
PF01421 (Reprolysin)
[Graphical view]


UniProtKB:Accession NumberP15167
Entry nameVMATD_CROAT
ActivityCleavage of 5-His-|-Leu-6, 10-His-|-Leu-11, 14-Ala-|-Leu-15, 16-Tyr-|-Leu-17 and 23-Gly-|-Phe-24 of insulin B chain. With small molecule substrates prefers hydrophobic residue at P2'' and small residue such as Ala, Gly at P1.
Subunit
Subcellular locationSecreted.
CofactorBinds 1 calcium ion per subunit.,Binds 1 zinc ion per subunit.

Compound table: links to PDB-related databases & PoSSuM

CofactorsSubstratesProducts
KEGG-idC00038C00017C00012C00001C00017C00012
CompoundZincProteinPeptideH2OProteinPeptide
Typeheavy metalpeptide/proteinpeptide/proteinH2Opeptide/proteinpeptide/protein
ChEBI29105


15377


PubChem32051


962
22247451


              
1atlABound:_ZNUnboundUnbound UnboundUnbound
1atlBBound:_ZNUnboundUnbound UnboundUnbound
1dthABound:_ZNUnboundUnbound UnboundUnbound
1dthBBound:_ZNUnboundUnbound UnboundUnbound
1htdABound:_ZNUnboundUnbound UnboundUnbound
1htdBBound:_ZNUnboundUnbound UnboundUnbound

Active-site residues
pdbCatalytic residuesCofactor-binding residues
          
1atlAGLU 143
HIS 142;HIS 146;HIS 152(Zinc binding)
1atlBGLU 143
HIS 142;HIS 146;HIS 152(Zinc binding)
1dthAGLU 143
HIS 142;HIS 146;HIS 152(Zinc binding)
1dthBGLU 143
HIS 142;HIS 146;HIS 152(Zinc binding)
1htdAGLU 143
HIS 142;HIS 146;HIS 152(Zinc binding)
1htdBGLU 143
HIS 142;HIS 146;HIS 152(Zinc binding)

References for Catalytic Mechanism
ReferencesSectionsNo. of steps in catalysis
[1]


references
[1]
CommentsX-ray crystallography
Medline ID94359948
PubMed ID8078901
JournalProc Natl Acad Sci U S A
Year1994
Volume91
Pages8447-51
AuthorsZhang D, Botos I, Gomis-Ruth FX, Doll R, Blood C, Njoroge FG, Fox JW, Bode W, Meyer EF
TitleStructural interaction of natural and synthetic inhibitors with the venom metalloproteinase, atrolysin C (form d).
Related PDB1atl,1htd
Related UniProtKBP15167
[2]
CommentsX-ray crystallography (2.0 Angstroms)
PubMed ID8610113
JournalProc Natl Acad Sci U S A
Year1996
Volume93
Pages2749-54
AuthorsBotos I, Scapozza L, Zhang D, Liotta LA, Meyer EF
TitleBatimastat, a potent matrix mealloproteinase inhibitor, exhibits an unexpected mode of binding.
Related PDB1dth
[3]
CommentsX-ray crystallography
PubMed ID12071970
JournalEur J Biochem
Year2002
Volume269
Pages3047-56
AuthorsHuang KF, Chiou SH, Ko TP, Wang AH
TitleDeterminants of the inhibition of a Taiwan habu venom metalloproteinase by its endogenous inhibitors revealed by X-ray crystallography and synthetic inhibitor analogues.

comments
This enzyme belongs to the peptidase family-M12B.
The zinc ion is catalytic in this enzyme (see [1]).

createdupdated
2002-09-122009-02-26


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Funded by BIRD/Japan Science and Technology Corporation (JST) (October 2007 - September 2010)
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