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SummaryStructural detailsExperimental detailsFunctional detailsSequence NeighborHistoryDownloads

1GXD

proMMP-2/TIMP-2 complex

Functional Information from GO Data
ChainGOidnamespacecontents
A0001525biological_processangiogenesis
A0001541biological_processovarian follicle development
A0001542biological_processovulation from ovarian follicle
A0001553biological_processluteinization
A0001666biological_processresponse to hypoxia
A0001968molecular_functionfibronectin binding
A0004175molecular_functionendopeptidase activity
A0004222molecular_functionmetalloendopeptidase activity
A0004252molecular_functionserine-type endopeptidase activity
A0005515molecular_functionprotein binding
A0005576cellular_componentextracellular region
A0005615cellular_componentextracellular space
A0005634cellular_componentnucleus
A0005737cellular_componentcytoplasm
A0005739cellular_componentmitochondrion
A0005886cellular_componentplasma membrane
A0006508biological_processproteolysis
A0006979biological_processresponse to oxidative stress
A0007162biological_processnegative regulation of cell adhesion
A0007507biological_processheart development
A0007565biological_processfemale pregnancy
A0007567biological_processparturition
A0008233molecular_functionpeptidase activity
A0008237molecular_functionmetallopeptidase activity
A0008270molecular_functionzinc ion binding
A0009410biological_processresponse to xenobiotic stimulus
A0009612biological_processresponse to mechanical stimulus
A0014012biological_processperipheral nervous system axon regeneration
A0014823biological_processresponse to activity
A0016020cellular_componentmembrane
A0016477biological_processcell migration
A0016787molecular_functionhydrolase activity
A0022617biological_processextracellular matrix disassembly
A0030017cellular_componentsarcomere
A0030163biological_processprotein catabolic process
A0030198biological_processextracellular matrix organization
A0030335biological_processpositive regulation of cell migration
A0030574biological_processcollagen catabolic process
A0031012cellular_componentextracellular matrix
A0032526biological_processresponse to retinoic acid
A0034097biological_processresponse to cytokine
A0035094biological_processresponse to nicotine
A0035987biological_processendodermal cell differentiation
A0042542biological_processresponse to hydrogen peroxide
A0043065biological_processpositive regulation of apoptotic process
A0043627biological_processresponse to estrogen
A0045906biological_processnegative regulation of vasoconstriction
A0046872molecular_functionmetal ion binding
A0048013biological_processephrin receptor signaling pathway
A0048246biological_processmacrophage chemotaxis
A0048771biological_processtissue remodeling
A0051602biological_processresponse to electrical stimulus
A0055093biological_processresponse to hyperoxia
A0060740biological_processprostate gland epithelium morphogenesis
A0061450biological_processtrophoblast cell migration
A0071345biological_processcellular response to cytokine stimulus
A0071347biological_processcellular response to interleukin-1
A0071392biological_processcellular response to estradiol stimulus
A0071492biological_processcellular response to UV-A
A0071498biological_processcellular response to fluid shear stress
A1903378biological_processpositive regulation of oxidative stress-induced neuron intrinsic apoptotic signaling pathway
A1904645biological_processresponse to amyloid-beta
A1904707biological_processpositive regulation of vascular associated smooth muscle cell proliferation
B0001525biological_processangiogenesis
B0001541biological_processovarian follicle development
B0001542biological_processovulation from ovarian follicle
B0001553biological_processluteinization
B0001666biological_processresponse to hypoxia
B0001968molecular_functionfibronectin binding
B0004175molecular_functionendopeptidase activity
B0004222molecular_functionmetalloendopeptidase activity
B0004252molecular_functionserine-type endopeptidase activity
B0005515molecular_functionprotein binding
B0005576cellular_componentextracellular region
B0005615cellular_componentextracellular space
B0005634cellular_componentnucleus
B0005737cellular_componentcytoplasm
B0005739cellular_componentmitochondrion
B0005886cellular_componentplasma membrane
B0006508biological_processproteolysis
B0006979biological_processresponse to oxidative stress
B0007162biological_processnegative regulation of cell adhesion
B0007507biological_processheart development
B0007565biological_processfemale pregnancy
B0007567biological_processparturition
B0008233molecular_functionpeptidase activity
B0008237molecular_functionmetallopeptidase activity
B0008270molecular_functionzinc ion binding
B0009410biological_processresponse to xenobiotic stimulus
B0009612biological_processresponse to mechanical stimulus
B0014012biological_processperipheral nervous system axon regeneration
B0014823biological_processresponse to activity
B0016020cellular_componentmembrane
B0016477biological_processcell migration
B0016787molecular_functionhydrolase activity
B0022617biological_processextracellular matrix disassembly
B0030017cellular_componentsarcomere
B0030163biological_processprotein catabolic process
B0030198biological_processextracellular matrix organization
B0030335biological_processpositive regulation of cell migration
B0030574biological_processcollagen catabolic process
B0031012cellular_componentextracellular matrix
B0032526biological_processresponse to retinoic acid
B0034097biological_processresponse to cytokine
B0035094biological_processresponse to nicotine
B0035987biological_processendodermal cell differentiation
B0042542biological_processresponse to hydrogen peroxide
B0043065biological_processpositive regulation of apoptotic process
B0043627biological_processresponse to estrogen
B0045906biological_processnegative regulation of vasoconstriction
B0046872molecular_functionmetal ion binding
B0048013biological_processephrin receptor signaling pathway
B0048246biological_processmacrophage chemotaxis
B0048771biological_processtissue remodeling
B0051602biological_processresponse to electrical stimulus
B0055093biological_processresponse to hyperoxia
B0060740biological_processprostate gland epithelium morphogenesis
B0061450biological_processtrophoblast cell migration
B0071345biological_processcellular response to cytokine stimulus
B0071347biological_processcellular response to interleukin-1
B0071392biological_processcellular response to estradiol stimulus
B0071492biological_processcellular response to UV-A
B0071498biological_processcellular response to fluid shear stress
B1903378biological_processpositive regulation of oxidative stress-induced neuron intrinsic apoptotic signaling pathway
B1904645biological_processresponse to amyloid-beta
B1904707biological_processpositive regulation of vascular associated smooth muscle cell proliferation
C0002020molecular_functionprotease binding
C0004857molecular_functionenzyme inhibitor activity
C0005515molecular_functionprotein binding
C0005576cellular_componentextracellular region
C0005615cellular_componentextracellular space
C0008191molecular_functionmetalloendopeptidase inhibitor activity
C0008270molecular_functionzinc ion binding
C0009725biological_processresponse to hormone
C0030414molecular_functionpeptidase inhibitor activity
C0031012cellular_componentextracellular matrix
C0034097biological_processresponse to cytokine
C0034774cellular_componentsecretory granule lumen
C0035580cellular_componentspecific granule lumen
C0045861biological_processnegative regulation of proteolysis
C0046872molecular_functionmetal ion binding
C0051045biological_processnegative regulation of membrane protein ectodomain proteolysis
C0140678molecular_functionmolecular function inhibitor activity
C1904724cellular_componenttertiary granule lumen
C1904813cellular_componentficolin-1-rich granule lumen
C1905049biological_processnegative regulation of metallopeptidase activity
D0002020molecular_functionprotease binding
D0004857molecular_functionenzyme inhibitor activity
D0005515molecular_functionprotein binding
D0005576cellular_componentextracellular region
D0005615cellular_componentextracellular space
D0008191molecular_functionmetalloendopeptidase inhibitor activity
D0008270molecular_functionzinc ion binding
D0009725biological_processresponse to hormone
D0030414molecular_functionpeptidase inhibitor activity
D0031012cellular_componentextracellular matrix
D0034097biological_processresponse to cytokine
D0034774cellular_componentsecretory granule lumen
D0035580cellular_componentspecific granule lumen
D0045861biological_processnegative regulation of proteolysis
D0046872molecular_functionmetal ion binding
D0051045biological_processnegative regulation of membrane protein ectodomain proteolysis
D0140678molecular_functionmolecular function inhibitor activity
D1904724cellular_componenttertiary granule lumen
D1904813cellular_componentficolin-1-rich granule lumen
D1905049biological_processnegative regulation of metallopeptidase activity
Functional Information from PDB Data
site_idAC1
Number of Residues4
DetailsBINDING SITE FOR RESIDUE SO4 A 1632
ChainResidue
AGLN269
AGLY270
ATHR271
BTHR278
site_idAC2
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ZN A 1633
ChainResidue
AHIS149
AASP151
AHIS164
AHIS177
site_idAC3
Number of Residues5
DetailsBINDING SITE FOR RESIDUE ZN A 1634
ChainResidue
AASN75
AHIS374
AHIS378
AHIS384
ACYS73
site_idAC4
Number of Residues6
DetailsBINDING SITE FOR RESIDUE CA A 1635
ChainResidue
AASP156
AGLY157
AASP159
ALEU161
AASP179
AGLU182
site_idAC5
Number of Residues4
DetailsBINDING SITE FOR RESIDUE SO4 B 1632
ChainResidue
ATHR278
BGLN269
BGLY270
BTHR271
site_idAC6
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ZN B 1633
ChainResidue
BHIS149
BASP151
BHIS164
BHIS177
site_idAC7
Number of Residues5
DetailsBINDING SITE FOR RESIDUE ZN B 1634
ChainResidue
BCYS73
BASN75
BHIS374
BHIS378
BHIS384
site_idAC8
Number of Residues6
DetailsBINDING SITE FOR RESIDUE CA B 1635
ChainResidue
BASP156
BGLY157
BASP159
BLEU161
BASP179
BGLU182
Functional Information from PROSITE/UniProt
site_idPS00023
Number of Residues42
DetailsFN2_1 Fibronectin type-II collagen-binding domain signature. CkfPFlFngkeynsCtdtgrsdgflWCsttyNFekdgkYgFC
ChainResidueDetails
ACYS204-CYS245
ACYS262-CYS303
ACYS320-CYS361
site_idPS00024
Number of Residues16
DetailsHEMOPEXIN Hemopexin domain signature. IAdaWnaiPdNLDAVV
ChainResidueDetails
AILE577-VAL592
site_idPS00288
Number of Residues13
DetailsTIMP Tissue inhibitors of metalloproteinases signature. CsCsPvHPQqaFC
ChainResidueDetails
CCYS1-CYS13
site_idPS00546
Number of Residues8
DetailsCYSTEINE_SWITCH Matrixins cysteine switch. PRCGnPDV
ChainResidueDetails
APRO71-VAL78
Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues79
DetailsPropeptide: {"description":"Activation peptide","featureId":"PRO_0000028714"}
ChainResidueDetails
site_idSWS_FT_FI2
Number of Residues96
DetailsDomain: {"description":"Fibronectin type-II 1","evidences":[{"source":"PROSITE-ProRule","id":"PRU00479","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails
site_idSWS_FT_FI3
Number of Residues96
DetailsDomain: {"description":"Fibronectin type-II 2","evidences":[{"source":"PROSITE-ProRule","id":"PRU00479","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails
site_idSWS_FT_FI4
Number of Residues96
DetailsDomain: {"description":"Fibronectin type-II 3","evidences":[{"source":"PROSITE-ProRule","id":"PRU00479","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails
site_idSWS_FT_FI5
Number of Residues88
DetailsRepeat: {"description":"Hemopexin 1"}
ChainResidueDetails
site_idSWS_FT_FI6
Number of Residues92
DetailsRepeat: {"description":"Hemopexin 2"}
ChainResidueDetails
site_idSWS_FT_FI7
Number of Residues96
DetailsRepeat: {"description":"Hemopexin 3"}
ChainResidueDetails
site_idSWS_FT_FI8
Number of Residues92
DetailsRepeat: {"description":"Hemopexin 4"}
ChainResidueDetails
site_idSWS_FT_FI9
Number of Residues222
DetailsRegion: {"description":"Collagenase-like 1"}
ChainResidueDetails
site_idSWS_FT_FI10
Number of Residues348
DetailsRegion: {"description":"Collagen-binding"}
ChainResidueDetails
site_idSWS_FT_FI11
Number of Residues14
DetailsMotif: {"description":"Cysteine switch","evidences":[{"evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI12
Number of Residues2
DetailsActive site: {"evidences":[{"source":"PROSITE-ProRule","id":"PRU10095","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"10356396","evidenceCode":"ECO:0000305"}]}
ChainResidueDetails
site_idSWS_FT_FI13
Number of Residues2
DetailsBinding site: {"description":"in inhibited form","evidences":[{"source":"PubMed","id":"10356396","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"12032297","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1CK7","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1EAK","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1GXD","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI14
Number of Residues4
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_FI15
Number of Residues4
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_FI16
Number of Residues8
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_FI17
Number of Residues12
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"21813640","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"3AYU","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI18
Number of Residues6
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
site_idSWS_FT_FI19
Number of Residues8
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"10356396","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"8549817","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1CK7","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1RTG","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI20
Number of Residues4
DetailsGlycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"evidenceCode":"ECO:0000255"}]}
ChainResidueDetails
site_idSWS_FT_FI21
Number of Residues250
DetailsDomain: {"description":"NTR","evidences":[{"source":"PROSITE-ProRule","id":"PRU00295","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails
site_idSWS_FT_FI22
Number of Residues8
DetailsRegion: {"description":"Involved in metalloproteinase-binding","evidences":[{"source":"PubMed","id":"24073280","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"4ILW","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI23
Number of Residues2
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"24073280","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"4ILW","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI24
Number of Residues6
DetailsSite: {"description":"Involved in metalloproteinase-binding","evidences":[{"source":"PubMed","id":"24073280","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"4ILW","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
Catalytic Information from CSA
site_idCSA1
Number of Residues2
DetailsAnnotated By Reference To The Literature 1hfs
ChainResidueDetails
AALA375
AMET392
site_idCSA2
Number of Residues2
DetailsAnnotated By Reference To The Literature 1hfs
ChainResidueDetails
BALA375
BMET392
site_idCSA3
Number of Residues1
DetailsAnnotated By Reference To The Literature 1hfs
ChainResidueDetails
ALYS195
site_idCSA4
Number of Residues1
DetailsAnnotated By Reference To The Literature 1hfs
ChainResidueDetails
AALA375
site_idCSA5
Number of Residues1
DetailsAnnotated By Reference To The Literature 1hfs
ChainResidueDetails
BLYS195
site_idCSA6
Number of Residues1
DetailsAnnotated By Reference To The Literature 1hfs
ChainResidueDetails
BALA375
site_idCSA7
Number of Residues1
DetailsAnnotated By Reference To The Literature 1hfs
ChainResidueDetails
AGLU202
site_idCSA8
Number of Residues1
DetailsAnnotated By Reference To The Literature 1hfs
ChainResidueDetails
BGLU202
site_idMCSA1
Number of Residues4
DetailsM-CSA 906
ChainResidueDetails
AHIS374metal ligand
AALA375proton shuttle (general acid/base)
AHIS378metal ligand
AHIS384metal ligand
site_idMCSA2
Number of Residues4
DetailsM-CSA 906
ChainResidueDetails
BHIS374metal ligand
BALA375proton shuttle (general acid/base)
BHIS378metal ligand
BHIS384metal ligand

250359

PDB entries from 2026-03-11

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