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1CK7

GELATINASE A (FULL-LENGTH)

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
Functional Information from PDB Data
site_idAC1
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ZN A 990
ChainResidue
ACYS102
AHIS403
AHIS407
AHIS413

site_idAC2
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ZN A 991
ChainResidue
AHIS178
AASP180
AHIS193
AHIS206

site_idAC3
Number of Residues6
DetailsBINDING SITE FOR RESIDUE CA A 992
ChainResidue
AASP185
AGLY186
AASP188
ALEU190
AASP208
AGLU211

site_idAC4
Number of Residues6
DetailsBINDING SITE FOR RESIDUE CA A 993
ChainResidue
AGLU166
AALA167
AASP168
AGLY200
AGLY202
AASP204

site_idAC5
Number of Residues4
DetailsBINDING SITE FOR RESIDUE CA A 994
ChainResidue
AASP476
AASP521
AASP569
AASP618

site_idAC6
Number of Residues4
DetailsBINDING SITE FOR RESIDUE CL A 995
ChainResidue
AALA522
AVAL523
AALA571
ANA996

site_idAC7
Number of Residues6
DetailsBINDING SITE FOR RESIDUE NA A 996
ChainResidue
AILE478
AALA479
AVAL523
AALA571
AVAL620
ACL995

site_idAC8
Number of Residues7
DetailsBINDING SITE FOR RESIDUE SO4 A 777
ChainResidue
AGLN52
ATYR53
ATHR56
APHE57
AASP185
ALEU190
AHOH1097

site_idAC9
Number of Residues4
DetailsBINDING SITE FOR RESIDUE SO4 A 778
ChainResidue
AGLN298
AGLY299
ATHR300
ATHR307

site_idCAA
Number of Residues6
DetailsCA 992 CATALYTIC DOMAIN
ChainResidue
AGLY186
AASP188
ALEU190
AASP208
AGLU211
AASP185

site_idCAB
Number of Residues6
DetailsCA 993 CATALYTIC DOMAIN
ChainResidue
AGLU166
AALA167
AASP168
AGLY200
AGLY202
AASP204

site_idCAH
Number of Residues4
DetailsCA 994 HEMOPEXIN DOMAIN
ChainResidue
AASP476
AASP521
AASP569
AASP618

site_idZNA
Number of Residues4
DetailsZN 990 ACTIVE SITE
ChainResidue
ACYS102
AHIS403
AHIS407
AHIS413

site_idZNS
Number of Residues4
DetailsZN 991 STRUCTURAL SITE
ChainResidue
AASP180
AHIS178
AHIS193
AHIS206

Functional Information from PROSITE/UniProt
site_idPS00023
Number of Residues42
DetailsFN2_1 Fibronectin type-II collagen-binding domain signature. CkfPFlFngkeynsCtdtgrsdgflWCsttyNFekdgkYgFC
ChainResidueDetails
ACYS233-CYS274
ACYS291-CYS332
ACYS349-CYS390

site_idPS00024
Number of Residues16
DetailsHEMOPEXIN Hemopexin domain signature. IAdaWnaiPdNLDAVV
ChainResidueDetails
AILE606-VAL621

site_idPS00546
Number of Residues8
DetailsCYSTEINE_SWITCH Matrixins cysteine switch. PRCGnPDV
ChainResidueDetails
APRO100-VAL107

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsACT_SITE: ACT_SITE => ECO:0000255|PROSITE-ProRule:PRU10095, ECO:0000305|PubMed:10356396
ChainResidueDetails
AALA404

site_idSWS_FT_FI2
Number of Residues1
DetailsBINDING: in inhibited form => ECO:0000269|PubMed:10356396, ECO:0000269|PubMed:12032297, ECO:0007744|PDB:1CK7, ECO:0007744|PDB:1EAK, ECO:0007744|PDB:1GXD
ChainResidueDetails
ACYS102

site_idSWS_FT_FI3
Number of Residues2
DetailsBINDING: BINDING => ECO:0000269|PubMed:21813640, ECO:0007744|PDB:1QIB, ECO:0007744|PDB:3AYU
ChainResidueDetails
AASP134
AASP209

site_idSWS_FT_FI4
Number of Residues2
DetailsBINDING: BINDING => ECO:0000269|PubMed:21813640, ECO:0007744|PDB:1EAK, ECO:0007744|PDB:3AYU
ChainResidueDetails
AASP168
AGLY200

site_idSWS_FT_FI5
Number of Residues4
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
AHIS178
AASP180
AHIS193
AHIS206

site_idSWS_FT_FI6
Number of Residues6
DetailsBINDING: BINDING => ECO:0000269|PubMed:21813640, ECO:0007744|PDB:3AYU
ChainResidueDetails
AASP185
AGLY186
AGLY202
AASP204
AASP208
AGLU211

site_idSWS_FT_FI7
Number of Residues3
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
AHIS403
AHIS407
AHIS413

site_idSWS_FT_FI8
Number of Residues4
DetailsBINDING: BINDING => ECO:0000269|PubMed:10356396, ECO:0000269|PubMed:8549817, ECO:0007744|PDB:1CK7, ECO:0007744|PDB:1RTG
ChainResidueDetails
AASP476
AASP521
AASP569
AASP618

site_idSWS_FT_FI9
Number of Residues2
DetailsCARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000255
ChainResidueDetails
AASN573
AASN642

Catalytic Information from CSA
site_idCSA1
Number of Residues1
Detailsa catalytic site defined by CSA, PubMed 9785958, 12401069
ChainResidueDetails
AALA404

site_idMCSA1
Number of Residues4
DetailsM-CSA 906
ChainResidueDetails
AHIS403metal ligand
AALA404proton shuttle (general acid/base)
AHIS407metal ligand
AHIS413metal ligand

224572

PDB entries from 2024-09-04

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