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3GBO

Crystal structure of BmooMPalpha-I, a non-hemorrhagic metalloproteinase isolated from Bothrops moojeni snake venom

Functional Information from GO Data
ChainGOidnamespacecontents
A0004222molecular_functionmetalloendopeptidase activity
A0005576cellular_componentextracellular region
A0005886cellular_componentplasma membrane
A0006508biological_processproteolysis
A0008233molecular_functionpeptidase activity
A0008237molecular_functionmetallopeptidase activity
A0016787molecular_functionhydrolase activity
A0035821biological_processmodulation of process of another organism
A0046872molecular_functionmetal ion binding
A0090729molecular_functiontoxin activity
Functional Information from PDB Data
site_idAC1
Number of Residues6
DetailsBINDING SITE FOR RESIDUE CA A 301
ChainResidue
AGLU7
AASP91
ACYS195
AASN198
AHOH405
AHOH410

site_idAC2
Number of Residues6
DetailsBINDING SITE FOR RESIDUE ZN A 302
ChainResidue
AHOH531
AHOH543
AHOH544
AHIS140
AHIS144
AHIS150

Functional Information from PROSITE/UniProt
site_idPS00142
Number of Residues10
DetailsZINC_PROTEASE Neutral zinc metallopeptidases, zinc-binding region signature. TMAHELGHNL
ChainResidueDetails
ATHR137-LEU146

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues196
DetailsDomain: {"description":"Peptidase M12B","evidences":[{"source":"PROSITE-ProRule","id":"PRU00276","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues1
DetailsActive site: {"evidences":[{"source":"UniProtKB","id":"P83512","evidenceCode":"ECO:0000250"},{"source":"PROSITE-ProRule","id":"PRU00276","evidenceCode":"ECO:0000255"},{"source":"PROSITE-ProRule","id":"PRU10095","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues7
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"19706302","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"3GBO","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

248636

PDB entries from 2026-02-04

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