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6BTP

BMP1 complexed with a hydroxamate

Functional Information from GO Data
ChainGOidnamespacecontents
A0004222molecular_functionmetalloendopeptidase activity
A0006508biological_processproteolysis
A0008237molecular_functionmetallopeptidase activity
A0008270molecular_functionzinc ion binding
B0004222molecular_functionmetalloendopeptidase activity
B0006508biological_processproteolysis
B0008237molecular_functionmetallopeptidase activity
B0008270molecular_functionzinc ion binding
Functional Information from PDB Data
site_idAC1
Number of Residues5
Detailsbinding site for residue SCN A 301
ChainResidue
AARG110
AILE116
AHOH468
AHOH492
BPHE162

site_idAC2
Number of Residues5
Detailsbinding site for residue ZN A 302
ChainResidue
AHOH450
AHIS93
AHIS97
AHIS103
AE8J304

site_idAC3
Number of Residues6
Detailsbinding site for residue ZN A 303
ChainResidue
AACE-1
AGLU104
AGLN192
AHOH410
AHOH425
AHOH438

site_idAC4
Number of Residues14
Detailsbinding site for residue E8J A 304
ChainResidue
ACYS66
ASER67
ATYR68
AVAL69
AHIS93
AGLU94
AHIS97
ATRP102
AHIS103
AGLN125
ATYR127
AZN302
AHOH450
BVAL175

site_idAC5
Number of Residues6
Detailsbinding site for residue SCN B 301
ChainResidue
BARG110
BPHE129
BLEU130
BHOH440
BHOH514
BHOH601

site_idAC6
Number of Residues5
Detailsbinding site for residue SCN B 302
ChainResidue
BARG8
BARG61
BPRO62
BTYR68
BVAL69

site_idAC7
Number of Residues4
Detailsbinding site for residue SCN B 303
ChainResidue
BTHR24
BPRO108
BASP109
BHOH530

site_idAC8
Number of Residues5
Detailsbinding site for residue ZN B 304
ChainResidue
BHIS93
BHIS97
BHIS103
BHOH529
BHOH564

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 Residues2
DetailsACT_SITE: ACT_SITE => ECO:0000255|PROSITE-ProRule:PRU01211, ECO:0000269|PubMed:18824173
ChainResidueDetails
AGLU94
BGLU94

site_idSWS_FT_FI2
Number of Residues6
DetailsBINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU01211, ECO:0000269|PubMed:18824173
ChainResidueDetails
AHIS93
AHIS97
AHIS103
BHIS93
BHIS97
BHIS103

site_idSWS_FT_FI3
Number of Residues2
DetailsCARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000255
ChainResidueDetails
AASN22
BASN22

222624

PDB entries from 2024-07-17

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