Loading
PDBj
MenuPDBj@FacebookPDBj@X(formerly Twitter)PDBj@BlueSkyPDBj@YouTubewwPDB FoundationwwPDBDonate
RCSB PDBPDBeBMRBAdv. SearchSearch help

3MA2

Complex membrane type-1 matrix metalloproteinase (MT1-MMP) with tissue inhibitor of metalloproteinase-1 (TIMP-1)

Functional Information from GO Data
ChainGOidnamespacecontents
A0004222molecular_functionmetalloendopeptidase activity
A0006508biological_processproteolysis
A0008237molecular_functionmetallopeptidase activity
A0008270molecular_functionzinc ion binding
A0031012cellular_componentextracellular matrix
B0008191molecular_functionmetalloendopeptidase inhibitor activity
C0008191molecular_functionmetalloendopeptidase inhibitor activity
D0004222molecular_functionmetalloendopeptidase activity
D0006508biological_processproteolysis
D0008237molecular_functionmetallopeptidase activity
D0008270molecular_functionzinc ion binding
D0031012cellular_componentextracellular matrix
Functional Information from PDB Data
site_idAC1
Number of Residues6
DetailsBINDING SITE FOR RESIDUE CA D 293
ChainResidue
DHOH23
DHOH26
DASP176
DASN208
DGLY210
DASP212

site_idAC2
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ZN D 294
ChainResidue
DHIS249
CCYS301
DHIS239
DHIS243

site_idAC3
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ZN D 295
ChainResidue
DHIS186
DASP188
DHIS201
DHIS214

site_idAC4
Number of Residues6
DetailsBINDING SITE FOR RESIDUE CA D 296
ChainResidue
DASP193
DGLY194
DGLY196
DPHE198
DASP216
DGLU219

site_idAC5
Number of Residues6
DetailsBINDING SITE FOR RESIDUE CA A 293
ChainResidue
AHOH64
AASP176
AASN208
AGLY210
AASP212
AHOH312

site_idAC6
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ZN A 294
ChainResidue
AHIS239
AHIS243
AHIS249
BCYS301

site_idAC7
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ZN A 295
ChainResidue
AHIS186
AASP188
AHIS201
AHIS214

site_idAC8
Number of Residues6
DetailsBINDING SITE FOR RESIDUE CA A 296
ChainResidue
AASP193
AGLY194
AGLY196
APHE198
AASP216
AGLU219

Functional Information from PROSITE/UniProt
site_idPS00142
Number of Residues10
DetailsZINC_PROTEASE Neutral zinc metallopeptidases, zinc-binding region signature. VAVHELGHAL
ChainResidueDetails
DVAL236-LEU245

site_idPS00288
Number of Residues13
DetailsTIMP Tissue inhibitors of metalloproteinases signature. CtCaPvHPQtaFC
ChainResidueDetails
BCYS301-CYS313

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsBINDING: BINDING => ECO:0000269|PubMed:22427646
ChainResidueDetails
BCYS301
CCYS301

site_idSWS_FT_FI2
Number of Residues2
DetailsSITE: Involved in metalloproteinase-binding => ECO:0000269|PubMed:22427646, ECO:0007744|PDB:3V96
ChainResidueDetails
BLEU334
DASP212
DHIS214
DASP216
DGLU219
DHIS239
DHIS243
DHIS249
AHIS186
AASP188
AASP193
CLEU334
AGLY194
AGLY196
APHE198
AHIS201
AASN208
AGLY210
AASP212
AHIS214
AASP216
AGLU219
DASP193
AHIS239
AHIS243
AHIS249
DGLY194
DGLY196
DPHE198
DHIS201
DASN208
DGLY210

site_idSWS_FT_FI3
Number of Residues2
DetailsCARBOHYD: N-linked (GlcNAc...) (complex) asparagine => ECO:0000269|PubMed:16263699, ECO:0000269|PubMed:16335952, ECO:0000269|PubMed:16740002, ECO:0000269|PubMed:19139490
ChainResidueDetails
BASN330
CASN330

site_idSWS_FT_FI4
Number of Residues2
DetailsCARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:16740002
ChainResidueDetails
BASN378
CASN378

237992

PDB entries from 2025-06-25

PDB statisticsPDBj update infoContact PDBjnumon