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3V96

Complex of matrix metalloproteinase-10 catalytic domain (MMP-10cd) with tissue inhibitor of metalloproteinases-1 (TIMP-1)

Functional Information from GO Data
ChainGOidnamespacecontents
A0002020molecular_functionprotease binding
A0002248biological_processconnective tissue replacement involved in inflammatory response wound healing
A0004857molecular_functionenzyme inhibitor activity
A0005125molecular_functioncytokine activity
A0005515molecular_functionprotein binding
A0005576cellular_componentextracellular region
A0005604cellular_componentbasement membrane
A0005615cellular_componentextracellular space
A0005788cellular_componentendoplasmic reticulum lumen
A0007165biological_processsignal transduction
A0008083molecular_functiongrowth factor activity
A0008191molecular_functionmetalloendopeptidase inhibitor activity
A0008270molecular_functionzinc ion binding
A0008284biological_processpositive regulation of cell population proliferation
A0009725biological_processresponse to hormone
A0010033biological_processresponse to organic substance
A0010951biological_processnegative regulation of endopeptidase activity
A0030414molecular_functionpeptidase inhibitor activity
A0031012cellular_componentextracellular matrix
A0031093cellular_componentplatelet alpha granule lumen
A0034097biological_processresponse to cytokine
A0043066biological_processnegative regulation of apoptotic process
A0043086biological_processnegative regulation of catalytic activity
A0043434biological_processresponse to peptide hormone
A0046872molecular_functionmetal ion binding
A0051045biological_processnegative regulation of membrane protein ectodomain proteolysis
A0051216biological_processcartilage development
A0070062cellular_componentextracellular exosome
A0071492biological_processcellular response to UV-A
A1901164biological_processnegative regulation of trophoblast cell migration
A1905049biological_processnegative regulation of metallopeptidase activity
A2001044biological_processregulation of integrin-mediated signaling pathway
B0004222molecular_functionmetalloendopeptidase activity
B0006508biological_processproteolysis
B0008237molecular_functionmetallopeptidase activity
B0008270molecular_functionzinc ion binding
B0031012cellular_componentextracellular matrix
Functional Information from PDB Data
site_idAC1
Number of Residues5
DetailsBINDING SITE FOR RESIDUE PO4 A 201
ChainResidue
AARG59
AARG162
AHIS163
AHOH351
AHOH371

site_idAC2
Number of Residues5
DetailsBINDING SITE FOR RESIDUE PO4 A 202
ChainResidue
AHOH370
ASER100
AVAL102
AGLU156
ALYS157

site_idAC3
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ZN B 301
ChainResidue
ACYS1
BHIS217
BHIS221
BHIS227

site_idAC4
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ZN B 302
ChainResidue
BHIS167
BASP169
BHIS182
BHIS195

site_idAC5
Number of Residues6
DetailsBINDING SITE FOR RESIDUE CA B 303
ChainResidue
BASP174
BGLY175
BGLY177
BSER179
BASP197
BGLU200

site_idAC6
Number of Residues6
DetailsBINDING SITE FOR RESIDUE CA B 304
ChainResidue
BASP157
BGLY189
BTYR191
BASP193
BHOH447
BHOH449

site_idAC7
Number of Residues3
DetailsBINDING SITE FOR RESIDUE CA B 305
ChainResidue
BASP123
BASP198
BGLU200

Functional Information from PROSITE/UniProt
site_idPS00142
Number of Residues10
DetailsZINC_PROTEASE Neutral zinc metallopeptidases, zinc-binding region signature. VAAHELGHSL
ChainResidueDetails
BVAL214-LEU223

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

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsACT_SITE: ACT_SITE => ECO:0000255|PROSITE-ProRule:PRU10095, ECO:0000269|PubMed:15095982
ChainResidueDetails
BGLU218

site_idSWS_FT_FI2
Number of Residues7
DetailsBINDING:
ChainResidueDetails
BHIS167
BASP169
BHIS182
BHIS195
BHIS217
BHIS221
BHIS227

site_idSWS_FT_FI3
Number of Residues1
DetailsMOD_RES: Phosphoserine; by FAM20C => ECO:0000269|PubMed:26091039
ChainResidueDetails
ASER155

site_idSWS_FT_FI4
Number of Residues1
DetailsCARBOHYD: N-linked (GlcNAc...) (complex) asparagine => ECO:0000269|PubMed:16263699, ECO:0000269|PubMed:16335952, ECO:0000269|PubMed:16740002, ECO:0000269|PubMed:19139490
ChainResidueDetails
AALA30

site_idSWS_FT_FI5
Number of Residues1
DetailsCARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:16740002
ChainResidueDetails
AASN78

218853

PDB entries from 2024-04-24

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