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6N9D

Complex of tissue inhibitor of metalloproteinases-1 (TIMP-1) mutant (L34G/L133P/L151C/G154A) with matrix metalloproteinase-3 catalytic domain (MMP-3cd)

Functional Information from GO Data
ChainGOidnamespacecontents
A0004222molecular_functionmetalloendopeptidase activity
A0006508biological_processproteolysis
A0008237molecular_functionmetallopeptidase activity
A0008270molecular_functionzinc ion binding
A0031012cellular_componentextracellular matrix
B0002020molecular_functionprotease binding
B0002248biological_processconnective tissue replacement involved in inflammatory response wound healing
B0004857molecular_functionenzyme inhibitor activity
B0005125molecular_functioncytokine activity
B0005515molecular_functionprotein binding
B0005576cellular_componentextracellular region
B0005604cellular_componentbasement membrane
B0005615cellular_componentextracellular space
B0005788cellular_componentendoplasmic reticulum lumen
B0007165biological_processsignal transduction
B0008083molecular_functiongrowth factor activity
B0008191molecular_functionmetalloendopeptidase inhibitor activity
B0008270molecular_functionzinc ion binding
B0008284biological_processpositive regulation of cell population proliferation
B0009725biological_processresponse to hormone
B0010033biological_processresponse to organic substance
B0010951biological_processnegative regulation of endopeptidase activity
B0030414molecular_functionpeptidase inhibitor activity
B0031012cellular_componentextracellular matrix
B0031093cellular_componentplatelet alpha granule lumen
B0034097biological_processresponse to cytokine
B0043066biological_processnegative regulation of apoptotic process
B0043086biological_processnegative regulation of catalytic activity
B0043434biological_processresponse to peptide hormone
B0046872molecular_functionmetal ion binding
B0051045biological_processnegative regulation of membrane protein ectodomain proteolysis
B0051216biological_processcartilage development
B0070062cellular_componentextracellular exosome
B0071492biological_processcellular response to UV-A
B1901164biological_processnegative regulation of trophoblast cell migration
B1905049biological_processnegative regulation of metallopeptidase activity
B2001044biological_processregulation of integrin-mediated signaling pathway
Functional Information from PDB Data
site_idAC1
Number of Residues6
Detailsbinding site for residue CA A 301
ChainResidue
AASP158
AGLY159
AGLY161
AVAL163
AASP181
AGLU184

site_idAC2
Number of Residues4
Detailsbinding site for residue CA A 302
ChainResidue
AGLU184
ATHR105
AASP107
AASP182

site_idAC3
Number of Residues4
Detailsbinding site for residue ZN A 303
ChainResidue
AHIS151
AASP153
AHIS166
AHIS179

site_idAC4
Number of Residues4
Detailsbinding site for residue ZN A 304
ChainResidue
AHIS201
AHIS205
AHIS211
BCYS1

site_idAC5
Number of Residues6
Detailsbinding site for residue CA A 305
ChainResidue
AALA140
AASP141
AGLY173
AASN175
AASP177
AHOH406

Functional Information from PROSITE/UniProt
site_idPS00142
Number of Residues10
DetailsZINC_PROTEASE Neutral zinc metallopeptidases, zinc-binding region signature. VAAHEIGHSL
ChainResidueDetails
AVAL198-LEU207

site_idPS00288
Number of Residues13
DetailsTIMP Tissue inhibitors of metalloproteinases signature. CtCvPpHPQtaFC
ChainResidueDetails
BCYS1-CYS13

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsBINDING: BINDING => ECO:0000269|PubMed:22427646
ChainResidueDetails
BCYS1

site_idSWS_FT_FI2
Number of Residues2
DetailsSITE: Involved in metalloproteinase-binding => ECO:0000269|PubMed:22427646, ECO:0007744|PDB:3V96
ChainResidueDetails
BGLY34
AGLY173
AASN175
AASP177
AHIS179
AASP181
AASP182
AGLU184
BILE135
AHIS151
AASP153
AASP158
AGLY159
AGLY161
AVAL163
AHIS166

site_idSWS_FT_FI3
Number of Residues1
DetailsMOD_RES: Phosphoserine; by FAM20C => ECO:0000269|PubMed:26091039
ChainResidueDetails
BSER155
AHIS205
AHIS211

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
BASN30

site_idSWS_FT_FI5
Number of Residues1
DetailsCARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:16740002
ChainResidueDetails
BASN78

Catalytic Information from CSA
site_idMCSA1
Number of Residues4
DetailsM-CSA 591
ChainResidueDetails
AHIS201metal ligand
AGLU202proton acceptor, proton donor
AHIS205metal ligand
AHIS211metal ligand

217705

PDB entries from 2024-03-27

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