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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
A0001955biological_processblood vessel maturation
A0001957biological_processintramembranous ossification
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
A0007566biological_processembryo implantation
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
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
A0034614biological_processcellular response to reactive oxygen species
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
A0048661biological_processpositive regulation of smooth muscle cell proliferation
A0048705biological_processskeletal system morphogenesis
A0048771biological_processtissue remodeling
A0051602biological_processresponse to electrical stimulus
A0055093biological_processresponse to hyperoxia
A0060325biological_processface morphogenesis
A0060346biological_processbone trabecula formation
A0060740biological_processprostate gland epithelium morphogenesis
A0062023cellular_componentcollagen-containing extracellular matrix
A0071230biological_processcellular response to amino acid stimulus
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
B0001955biological_processblood vessel maturation
B0001957biological_processintramembranous ossification
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
B0007566biological_processembryo implantation
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
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
B0034614biological_processcellular response to reactive oxygen species
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
B0048661biological_processpositive regulation of smooth muscle cell proliferation
B0048705biological_processskeletal system morphogenesis
B0048771biological_processtissue remodeling
B0051602biological_processresponse to electrical stimulus
B0055093biological_processresponse to hyperoxia
B0060325biological_processface morphogenesis
B0060346biological_processbone trabecula formation
B0060740biological_processprostate gland epithelium morphogenesis
B0062023cellular_componentcollagen-containing extracellular matrix
B0071230biological_processcellular response to amino acid stimulus
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
C0005515molecular_functionprotein binding
C0005576cellular_componentextracellular region
C0005615cellular_componentextracellular space
C0008191molecular_functionmetalloendopeptidase inhibitor activity
C0008270molecular_functionzinc ion binding
C0009725biological_processresponse to hormone
C0010466biological_processnegative regulation of peptidase activity
C0030414molecular_functionpeptidase inhibitor activity
C0031012cellular_componentextracellular matrix
C0034097biological_processresponse to cytokine
C0035580cellular_componentspecific granule lumen
C0046872molecular_functionmetal ion binding
C0051045biological_processnegative regulation of membrane protein ectodomain proteolysis
C0062023cellular_componentcollagen-containing extracellular matrix
C0140678molecular_functionmolecular function inhibitor activity
C1904724cellular_componenttertiary granule lumen
C1904813cellular_componentficolin-1-rich granule lumen
C1905049biological_processnegative regulation of metallopeptidase activity
D0002020molecular_functionprotease binding
D0005515molecular_functionprotein binding
D0005576cellular_componentextracellular region
D0005615cellular_componentextracellular space
D0008191molecular_functionmetalloendopeptidase inhibitor activity
D0008270molecular_functionzinc ion binding
D0009725biological_processresponse to hormone
D0010466biological_processnegative regulation of peptidase activity
D0030414molecular_functionpeptidase inhibitor activity
D0031012cellular_componentextracellular matrix
D0034097biological_processresponse to cytokine
D0035580cellular_componentspecific granule lumen
D0046872molecular_functionmetal ion binding
D0051045biological_processnegative regulation of membrane protein ectodomain proteolysis
D0062023cellular_componentcollagen-containing extracellular matrix
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 Residues2
DetailsBINDING: BINDING => ECO:0000269|PubMed:24073280, ECO:0007744|PDB:4ILW
ChainResidueDetails
CCYS1
DCYS1

site_idSWS_FT_FI2
Number of Residues6
DetailsSITE: Involved in metalloproteinase-binding => ECO:0000269|PubMed:24073280, ECO:0007744|PDB:4ILW
ChainResidueDetails
CASN14
CILE35
CLYS41
DASN14
DILE35
DLYS41

site_idSWS_FT_FI3
Number of Residues4
DetailsBINDING: BINDING => ECO:0000269|PubMed:21813640, ECO:0007744|PDB:1QIB, ECO:0007744|PDB:3AYU
ChainResidueDetails
AASP105
AASP180
BASP105
BASP180

site_idSWS_FT_FI4
Number of Residues4
DetailsBINDING: BINDING => ECO:0000269|PubMed:21813640, ECO:0007744|PDB:1EAK, ECO:0007744|PDB:3AYU
ChainResidueDetails
AASP139
AGLY171
BASP139
BGLY171

site_idSWS_FT_FI5
Number of Residues8
DetailsBINDING: BINDING => ECO:0000269|PubMed:10356396, ECO:0000269|PubMed:12032297, ECO:0000269|PubMed:21813640, ECO:0007744|PDB:1CK7, ECO:0007744|PDB:1EAK, ECO:0007744|PDB:1GXD, ECO:0007744|PDB:1QIB, ECO:0007744|PDB:3AYU
ChainResidueDetails
AHIS149
AASP151
AHIS164
AHIS177
BHIS149
BASP151
BHIS164
BHIS177

site_idSWS_FT_FI6
Number of Residues12
DetailsBINDING: BINDING => ECO:0000269|PubMed:21813640, ECO:0007744|PDB:3AYU
ChainResidueDetails
AASP156
BASP175
BASP179
BGLU182
AGLY157
AGLY173
AASP175
AASP179
AGLU182
BASP156
BGLY157
BGLY173

site_idSWS_FT_FI7
Number of Residues6
DetailsBINDING: BINDING => ECO:0000269|PubMed:10356396, ECO:0000269|PubMed:12032297, ECO:0000269|PubMed:21813640, ECO:0007744|PDB:1CK7, ECO:0007744|PDB:1EAK, ECO:0007744|PDB:1GXD, ECO:0007744|PDB:3AYU
ChainResidueDetails
AHIS374
AHIS378
AHIS384
BHIS374
BHIS378
BHIS384

site_idSWS_FT_FI8
Number of Residues8
DetailsBINDING: BINDING => ECO:0000269|PubMed:10356396, ECO:0000269|PubMed:8549817, ECO:0007744|PDB:1CK7, ECO:0007744|PDB:1RTG
ChainResidueDetails
AASP447
AASP492
AASP540
AASP589
BASP447
BASP492
BASP540
BASP589

site_idSWS_FT_FI9
Number of Residues4
DetailsCARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000255
ChainResidueDetails
AASN544
AASN613
BASN544
BASN613

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

224572

PDB entries from 2024-09-04

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