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SummaryStructural detailsExperimental detailsFunctional detailsSequence NeighborHistoryDownloads

1UEA

MMP-3/TIMP-1 COMPLEX

Functional Information from GO Data
ChainGOidnamespacecontents
A0004222molecular_functionmetalloendopeptidase activity
A0006508biological_processproteolysis
A0008237molecular_functionmetallopeptidase activity
A0008270molecular_functionzinc ion binding
A0031012cellular_componentextracellular matrix
B0002020molecular_functionprotease binding
B0002248biological_processconnective tissue replacement involved in inflammatory response wound healing
B0004857molecular_functionenzyme inhibitor activity
B0005125molecular_functioncytokine activity
B0005515molecular_functionprotein binding
B0005576cellular_componentextracellular region
B0005604cellular_componentbasement membrane
B0005615cellular_componentextracellular space
B0005788cellular_componentendoplasmic reticulum lumen
B0007165biological_processsignal transduction
B0008083molecular_functiongrowth factor activity
B0008191molecular_functionmetalloendopeptidase inhibitor activity
B0008270molecular_functionzinc ion binding
B0008284biological_processpositive regulation of cell population proliferation
B0009725biological_processresponse to hormone
B0010951biological_processnegative regulation of endopeptidase activity
B0030414molecular_functionpeptidase inhibitor activity
B0031012cellular_componentextracellular matrix
B0031093cellular_componentplatelet alpha granule lumen
B0034097biological_processresponse to cytokine
B0034774cellular_componentsecretory granule lumen
B0043066biological_processnegative regulation of apoptotic process
B0043086biological_processnegative regulation of catalytic activity
B0043434biological_processresponse to peptide hormone
B0045861biological_processnegative regulation of proteolysis
B0046872molecular_functionmetal ion binding
B0051045biological_processnegative regulation of membrane protein ectodomain proteolysis
B0051216biological_processcartilage development
B0070062cellular_componentextracellular exosome
B0071492biological_processcellular response to UV-A
B1901164biological_processnegative regulation of trophoblast cell migration
B1901653biological_processcellular response to peptide
B1905049biological_processnegative regulation of metallopeptidase activity
B1905641biological_processcellular response to acetaldehyde
B2001044biological_processregulation of integrin-mediated signaling pathway
C0004222molecular_functionmetalloendopeptidase activity
C0006508biological_processproteolysis
C0008237molecular_functionmetallopeptidase activity
C0008270molecular_functionzinc ion binding
C0031012cellular_componentextracellular matrix
D0002020molecular_functionprotease binding
D0002248biological_processconnective tissue replacement involved in inflammatory response wound healing
D0004857molecular_functionenzyme inhibitor activity
D0005125molecular_functioncytokine activity
D0005515molecular_functionprotein binding
D0005576cellular_componentextracellular region
D0005604cellular_componentbasement membrane
D0005615cellular_componentextracellular space
D0005788cellular_componentendoplasmic reticulum lumen
D0007165biological_processsignal transduction
D0008083molecular_functiongrowth factor activity
D0008191molecular_functionmetalloendopeptidase inhibitor activity
D0008270molecular_functionzinc ion binding
D0008284biological_processpositive regulation of cell population proliferation
D0009725biological_processresponse to hormone
D0010951biological_processnegative regulation of endopeptidase activity
D0030414molecular_functionpeptidase inhibitor activity
D0031012cellular_componentextracellular matrix
D0031093cellular_componentplatelet alpha granule lumen
D0034097biological_processresponse to cytokine
D0034774cellular_componentsecretory granule lumen
D0043066biological_processnegative regulation of apoptotic process
D0043086biological_processnegative regulation of catalytic activity
D0043434biological_processresponse to peptide hormone
D0045861biological_processnegative regulation of proteolysis
D0046872molecular_functionmetal ion binding
D0051045biological_processnegative regulation of membrane protein ectodomain proteolysis
D0051216biological_processcartilage development
D0070062cellular_componentextracellular exosome
D0071492biological_processcellular response to UV-A
D1901164biological_processnegative regulation of trophoblast cell migration
D1901653biological_processcellular response to peptide
D1905049biological_processnegative regulation of metallopeptidase activity
D1905641biological_processcellular response to acetaldehyde
D2001044biological_processregulation of integrin-mediated signaling pathway
Functional Information from PDB Data
site_idAC1
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ZN A 1
ChainResidue
AHIS201
AHIS205
AHIS211
BCYS1
site_idAC2
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ZN A 2
ChainResidue
AHIS151
AASP153
AHIS166
AHIS179
site_idAC3
Number of Residues6
DetailsBINDING SITE FOR RESIDUE CA A 3
ChainResidue
AGLY159
AGLY161
AVAL163
AASP181
AGLU184
AASP158
site_idAC4
Number of Residues4
DetailsBINDING SITE FOR RESIDUE CA A 4
ChainResidue
AASP141
AGLY173
AASN175
AASP177
site_idAC5
Number of Residues5
DetailsBINDING SITE FOR RESIDUE CA A 5
ChainResidue
AASP107
AASP182
AASP183
AGLU184
AHOH1337
site_idAC6
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ZN C 1
ChainResidue
CHIS201
CHIS205
CHIS211
DCYS1
site_idAC7
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ZN C 2
ChainResidue
CHIS151
CASP153
CHIS166
CHIS179
site_idAC8
Number of Residues6
DetailsBINDING SITE FOR RESIDUE CA C 3
ChainResidue
CASP158
CGLY159
CGLY161
CVAL163
CASP181
CGLU184
site_idAC9
Number of Residues5
DetailsBINDING SITE FOR RESIDUE CA C 4
ChainResidue
CALA140
CASP141
CGLY173
CASN175
CASP177
site_idBC1
Number of Residues4
DetailsBINDING SITE FOR RESIDUE CA C 5
ChainResidue
CASP107
CASP182
CGLU184
CGLN185
Functional Information from PROSITE/UniProt
site_idPS00142
Number of Residues10
DetailsZINC_PROTEASE Neutral zinc metallopeptidases, zinc-binding region signature. VAAHEIGHSL
ChainResidueDetails
AVAL198-LEU207
site_idPS00288
Number of Residues13
DetailsTIMP Tissue inhibitors of metalloproteinases signature. CtCvPpHPQtaFC
ChainResidueDetails
BCYS1-CYS13
Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsActive site: {}
ChainResidueDetails
site_idSWS_FT_FI2
Number of Residues32
DetailsBinding site: {}
ChainResidueDetails
site_idSWS_FT_FI3
Number of Residues6
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"8740360","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI4
Number of Residues246
DetailsDomain: {"description":"NTR","evidences":[{"source":"PROSITE-ProRule","id":"PRU00295","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails
site_idSWS_FT_FI5
Number of Residues10
DetailsRegion: {"description":"Involved in metalloproteinase-binding","evidences":[{"source":"PubMed","id":"22427646","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"3V96","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI6
Number of Residues2
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"22427646","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI7
Number of Residues4
DetailsSite: {"description":"Involved in metalloproteinase-binding","evidences":[{"source":"PubMed","id":"22427646","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"3V96","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI8
Number of Residues2
DetailsModified residue: {"description":"Phosphoserine; by FAM20C","evidences":[{"source":"PubMed","id":"26091039","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI9
Number of Residues2
DetailsGlycosylation: {"description":"N-linked (GlcNAc...) (complex) asparagine","featureId":"CAR_000002","evidences":[{"source":"PubMed","id":"16263699","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"16335952","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"16740002","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"19139490","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI10
Number of Residues2
DetailsGlycosylation: {"description":"N-linked (GlcNAc...) asparagine","featureId":"CAR_000003","evidences":[{"source":"PubMed","id":"16740002","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
Catalytic Information from CSA
site_idCSA1
Number of Residues1
DetailsAnnotated By Reference To The Literature 1hfs
ChainResidueDetails
AGLU202
site_idCSA2
Number of Residues1
DetailsAnnotated By Reference To The Literature 1hfs
ChainResidueDetails
CGLU202
site_idMCSA1
Number of Residues4
DetailsM-CSA 591
ChainResidueDetails
AHIS205metal ligand
ASER206proton acceptor, proton donor
ALEU209metal ligand
ATHR215metal ligand
site_idMCSA2
Number of Residues4
DetailsM-CSA 591
ChainResidueDetails
CHIS205metal ligand
CSER206proton acceptor, proton donor
CLEU209metal ligand
CTHR215metal ligand

243531

PDB entries from 2025-10-22

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