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6BSM

BMP1 complexed with a reverse hydroxamate - compound 4

Functional Information from GO Data
ChainGOidnamespacecontents
A0004222molecular_functionmetalloendopeptidase activity
A0006508biological_processproteolysis
A0008237molecular_functionmetallopeptidase activity
A0008270molecular_functionzinc ion binding
Functional Information from PDB Data
site_idAC1
Number of Residues4
Detailsbinding site for residue ZN A 301
ChainResidue
AHIS93
AHIS97
AHIS103
AE7D303

site_idAC2
Number of Residues6
Detailsbinding site for residue ZN A 302
ChainResidue
AHOH454
AACE-1
AGLU104
AGLN192
AHOH416
AHOH437

site_idAC3
Number of Residues16
Detailsbinding site for residue E7D A 303
ChainResidue
AGLY64
ACYS66
ASER67
ATYR68
AVAL69
AHIS93
AGLU94
AHIS97
ATRP102
AHIS103
APRO123
AARG159
ALEU163
AZN301
AHOH405
AHOH412

Functional Information from PROSITE/UniProt
site_idPS00142
Number of Residues10
DetailsZINC_PROTEASE Neutral zinc metallopeptidases, zinc-binding region signature. IVVHELGHVV
ChainResidueDetails
AILE90-VAL99

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsActive site: {"evidences":[{"source":"PROSITE-ProRule","id":"PRU01211","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"18824173","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues3
DetailsBinding site: {"evidences":[{"source":"PROSITE-ProRule","id":"PRU01211","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"18824173","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues1
DetailsGlycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

238895

PDB entries from 2025-07-16

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