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4ILW

Complex of matrix metalloproteinase-10 catalytic domain (MMP-10cd) with tissue inhibitor of metalloproteinases-2 (TIMP-2)

Functional Information from GO Data
ChainGOidnamespacecontents
A0002020molecular_functionprotease binding
A0004857molecular_functionenzyme inhibitor activity
A0005515molecular_functionprotein binding
A0005576cellular_componentextracellular region
A0005615cellular_componentextracellular space
A0008191molecular_functionmetalloendopeptidase inhibitor activity
A0008270molecular_functionzinc ion binding
A0009725biological_processresponse to hormone
A0030414molecular_functionpeptidase inhibitor activity
A0031012cellular_componentextracellular matrix
A0034097biological_processresponse to cytokine
A0034774cellular_componentsecretory granule lumen
A0035580cellular_componentspecific granule lumen
A0045861biological_processnegative regulation of proteolysis
A0046872molecular_functionmetal ion binding
A0051045biological_processnegative regulation of membrane protein ectodomain proteolysis
A0140678molecular_functionmolecular function inhibitor activity
A1904724cellular_componenttertiary granule lumen
A1904813cellular_componentficolin-1-rich granule lumen
A1905049biological_processnegative regulation of metallopeptidase activity
B0002020molecular_functionprotease binding
B0004857molecular_functionenzyme inhibitor activity
B0005515molecular_functionprotein binding
B0005576cellular_componentextracellular region
B0005615cellular_componentextracellular space
B0008191molecular_functionmetalloendopeptidase inhibitor activity
B0008270molecular_functionzinc ion binding
B0009725biological_processresponse to hormone
B0030414molecular_functionpeptidase inhibitor activity
B0031012cellular_componentextracellular matrix
B0034097biological_processresponse to cytokine
B0034774cellular_componentsecretory granule lumen
B0035580cellular_componentspecific granule lumen
B0045861biological_processnegative regulation of proteolysis
B0046872molecular_functionmetal ion binding
B0051045biological_processnegative regulation of membrane protein ectodomain proteolysis
B0140678molecular_functionmolecular function inhibitor activity
B1904724cellular_componenttertiary granule lumen
B1904813cellular_componentficolin-1-rich granule lumen
B1905049biological_processnegative regulation of metallopeptidase activity
D0004222molecular_functionmetalloendopeptidase activity
D0006508biological_processproteolysis
D0008237molecular_functionmetallopeptidase activity
D0008270molecular_functionzinc ion binding
D0031012cellular_componentextracellular matrix
F0004222molecular_functionmetalloendopeptidase activity
F0006508biological_processproteolysis
F0008237molecular_functionmetallopeptidase activity
F0008270molecular_functionzinc ion binding
F0031012cellular_componentextracellular matrix
Functional Information from PDB Data
site_idAC1
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ZN D 301
ChainResidue
ACYS1
DHIS217
DHIS221
DHIS227

site_idAC2
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ZN D 302
ChainResidue
DHIS167
DASP169
DHIS182
DHIS195

site_idAC3
Number of Residues6
DetailsBINDING SITE FOR RESIDUE CA D 303
ChainResidue
DGLY175
DGLY177
DSER179
DASP197
DGLU200
DASP174

site_idAC4
Number of Residues5
DetailsBINDING SITE FOR RESIDUE CA D 304
ChainResidue
DASP157
DGLY189
DTYR191
DASP193
DHOH410

site_idAC5
Number of Residues4
DetailsBINDING SITE FOR RESIDUE CA D 305
ChainResidue
DASP123
DASP198
DGLU200
DHOH425

site_idAC6
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ZN F 301
ChainResidue
BCYS1
FHIS217
FHIS221
FHIS227

site_idAC7
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ZN F 302
ChainResidue
FHIS167
FASP169
FHIS182
FHIS195

site_idAC8
Number of Residues6
DetailsBINDING SITE FOR RESIDUE CA F 303
ChainResidue
FASP174
FGLY175
FGLY177
FSER179
FASP197
FGLU200

site_idAC9
Number of Residues4
DetailsBINDING SITE FOR RESIDUE CA F 304
ChainResidue
FASP157
FGLY189
FTYR191
FASP193

site_idBC1
Number of Residues3
DetailsBINDING SITE FOR RESIDUE CA F 305
ChainResidue
FASP123
FASP198
FGLU200

Functional Information from PROSITE/UniProt
site_idPS00142
Number of Residues10
DetailsZINC_PROTEASE Neutral zinc metallopeptidases, zinc-binding region signature. VAAHELGHSL
ChainResidueDetails
DVAL214-LEU223

site_idPS00288
Number of Residues13
DetailsTIMP Tissue inhibitors of metalloproteinases signature. CsCsPvHPQqaFC
ChainResidueDetails
ACYS1-CYS13

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues250
DetailsDomain: {"description":"NTR","evidences":[{"source":"PROSITE-ProRule","id":"PRU00295","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI2
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_FI3
Number of Residues2
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"24073280","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"4ILW","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI4
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

site_idSWS_FT_FI5
Number of Residues2
DetailsActive site: {"evidences":[{"source":"PROSITE-ProRule","id":"PRU10095","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"15095982","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI6
Number of Residues14
DetailsBinding site: {}
ChainResidueDetails

246031

PDB entries from 2025-12-10

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