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1HOV

SOLUTION STRUCTURE OF A CATALYTIC DOMAIN OF MMP-2 COMPLEXED WITH SC-74020

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 165
ChainResidue
AHIS70
AASP72
AHIS85
AHIS98

site_idAC2
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ZN A 166
ChainResidue
AHIS120
AHIS124
AHIS130
AI52800

site_idAC3
Number of Residues7
DetailsBINDING SITE FOR RESIDUE CA A 167
ChainResidue
AGLY78
ALYS79
AASP80
ALEU82
AASP100
AGLU103
AASP77

site_idAC4
Number of Residues6
DetailsBINDING SITE FOR RESIDUE CA A 168
ChainResidue
AASP60
AGLY92
AVAL93
AGLY94
AGLY95
AASP96

site_idAC5
Number of Residues19
DetailsBINDING SITE FOR RESIDUE I52 A 800
ChainResidue
AGLY81
ALEU82
ALEU83
AALA84
AHIS85
AHIS120
AGLU121
AHIS124
AHIS130
AALA136
ALEU137
AALA139
AILE141
ATYR142
ATHR143
ATHR145
APHE148
AARG149
AZN166

Functional Information from PROSITE/UniProt
site_idPS00142
Number of Residues10
DetailsZINC_PROTEASE Neutral zinc metallopeptidases, zinc-binding region signature. VAAHEFGHAM
ChainResidueDetails
AVAL117-MET126

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsActive site: {"evidences":[{"source":"PROSITE-ProRule","id":"PRU10095","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"10356396","evidenceCode":"ECO:0000305"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues2
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"21813640","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1QIB","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3AYU","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues2
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"21813640","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1EAK","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3AYU","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues4
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"10356396","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"12032297","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"21813640","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1CK7","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1EAK","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1GXD","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1QIB","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3AYU","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI5
Number of Residues6
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"21813640","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"3AYU","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI6
Number of Residues3
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"10356396","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"12032297","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"21813640","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1CK7","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1EAK","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1GXD","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3AYU","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

Catalytic Information from CSA
site_idCSA1
Number of Residues2
DetailsAnnotated By Reference To The Literature 1hfs
ChainResidueDetails
AGLU121
AMET138

site_idCSA2
Number of Residues1
DetailsAnnotated By Reference To The Literature 1hfs
ChainResidueDetails
AGLU121

site_idMCSA1
Number of Residues4
DetailsM-CSA 906
ChainResidueDetails
AHIS120metal ligand
AGLU121proton shuttle (general acid/base)
AHIS124metal ligand
AHIS130metal ligand

247536

PDB entries from 2026-01-14

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