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1FM1

SOLUTION STRUCTURE OF THE CATALYTIC FRAGMENT OF HUMAN COLLAGENASE-3 (MMP-13) COMPLEXED WITH A HYDROXAMIC ACID INHIBITOR

Functional Information from GO Data
ChainGOidnamespacecontents
A0004222molecular_functionmetalloendopeptidase activity
A0006508biological_processproteolysis
A0008237molecular_functionmetallopeptidase activity
A0008270molecular_functionzinc ion binding
A0031012cellular_componentextracellular matrix
Functional Information from PDB Data
site_idAC1
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ZN A 166
ChainResidue
AHIS119
AHIS123
AHIS129
AWAY169

site_idAC2
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ZN A 167
ChainResidue
AHIS69
AASP71
AHIS84
AHIS97

site_idAC3
Number of Residues8
DetailsBINDING SITE FOR RESIDUE CA A 168
ChainResidue
AGLY77
APRO78
ASER79
AGLY80
ALEU81
AASP99
AGLU102
AASP76

site_idAC4
Number of Residues9
DetailsBINDING SITE FOR RESIDUE WAY A 169
ChainResidue
AGLY80
ALEU81
ALEU82
ALEU115
AHIS119
AHIS123
AHIS129
APRO139
AZN166

Functional Information from PROSITE/UniProt
site_idPS00142
Number of Residues10
DetailsZINC_PROTEASE Neutral zinc metallopeptidases, zinc-binding region signature. VAAHEFGHSL
ChainResidueDetails
AVAL116-LEU125

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsACT_SITE: ACT_SITE => ECO:0000305|PubMed:23913860
ChainResidueDetails
AGLU120

site_idSWS_FT_FI2
Number of Residues12
DetailsBINDING: BINDING => ECO:0000269|PubMed:10926524, ECO:0000269|PubMed:10986126, ECO:0000269|PubMed:15734645, ECO:0000269|PubMed:15780611, ECO:0000269|PubMed:17196980, ECO:0000269|PubMed:17623656, ECO:0000269|PubMed:19422229, ECO:0000269|PubMed:20005097, ECO:0000269|PubMed:20726512, ECO:0000269|PubMed:22689580, ECO:0000269|PubMed:23810497, ECO:0000269|PubMed:23913860, ECO:0000269|PubMed:8969305
ChainResidueDetails
AASP25
AASP99
AASP100
AGLU102
AASP59
AASP76
AGLY77
ASER79
ALEU81
AASN91
AGLY93
AASP95

site_idSWS_FT_FI3
Number of Residues8
DetailsBINDING: BINDING => ECO:0000269|PubMed:10926524, ECO:0000269|PubMed:10986126, ECO:0000269|PubMed:15734645, ECO:0000269|PubMed:15780611, ECO:0000269|PubMed:17196980, ECO:0000269|PubMed:17623656, ECO:0000269|PubMed:19422229, ECO:0000269|PubMed:20005097, ECO:0000269|PubMed:20726512, ECO:0000269|PubMed:22689580, ECO:0000269|PubMed:23810497, ECO:0000269|PubMed:23913860
ChainResidueDetails
AHIS69
AASP71
AHIS84
AHIS97
AHIS119
AHIS123
AHIS129
AMET137

site_idSWS_FT_FI4
Number of Residues1
DetailsCARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:8576151
ChainResidueDetails
AASN14

site_idSWS_FT_FI5
Number of Residues1
DetailsCARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000255
ChainResidueDetails
AASN49

Catalytic Information from CSA
site_idCSA1
Number of Residues2
DetailsAnnotated By Reference To The Literature 1hfs
ChainResidueDetails
AGLU120
AMET137

site_idCSA2
Number of Residues1
DetailsAnnotated By Reference To The Literature 1hfs
ChainResidueDetails
AGLU120

219140

PDB entries from 2024-05-01

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