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1BQQ

CRYSTAL STRUCTURE OF THE MT1-MMP--TIMP-2 COMPLEX

Functional Information from GO Data
ChainGOidnamespacecontents
M0004222molecular_functionmetalloendopeptidase activity
M0006508biological_processproteolysis
M0008237molecular_functionmetallopeptidase activity
M0008270molecular_functionzinc ion binding
M0031012cellular_componentextracellular matrix
T0004857molecular_functionenzyme inhibitor activity
T0005576cellular_componentextracellular region
T0005615cellular_componentextracellular space
T0008191molecular_functionmetalloendopeptidase inhibitor activity
T0009725biological_processresponse to hormone
T0030414molecular_functionpeptidase inhibitor activity
T0031012cellular_componentextracellular matrix
T0034097biological_processresponse to cytokine
T0046872molecular_functionmetal ion binding
T0051045biological_processnegative regulation of membrane protein ectodomain proteolysis
Functional Information from PDB Data
site_idAC1
Number of Residues4
DetailsBINDING SITE FOR RESIDUE CA M 288
ChainResidue
MASP176
MASN208
MGLY210
MASP212

site_idAC2
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ZN M 289
ChainResidue
MHIS239
MHIS243
MHIS249
TCYS1001

site_idAC3
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ZN M 290
ChainResidue
MASP188
MHIS201
MHIS214
MHIS186

site_idAC4
Number of Residues6
DetailsBINDING SITE FOR RESIDUE CA M 291
ChainResidue
MASP193
MGLY194
MGLY196
MPHE198
MASP216
MGLU219

Functional Information from PROSITE/UniProt
site_idPS00142
Number of Residues10
DetailsZINC_PROTEASE Neutral zinc metallopeptidases, zinc-binding region signature. VAVHELGHAL
ChainResidueDetails
MVAL236-LEU245

site_idPS00288
Number of Residues13
DetailsTIMP Tissue inhibitors of metalloproteinases signature. CsCsPvHPQqaFC
ChainResidueDetails
TCYS1001-CYS1013

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsActive site: {"evidences":[{"source":"PROSITE-ProRule","id":"PRU10095","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"35177851","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"9724659","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues16
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"9724659","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1BQQ","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1BUV","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues125
DetailsDomain: {"description":"NTR","evidences":[{"source":"PROSITE-ProRule","id":"PRU00295","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues3
DetailsRegion: {"description":"Involved in metalloproteinase-binding","evidences":[{"source":"PubMed","id":"17196980","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"2E2D","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI5
Number of Residues1
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"17196980","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"2E2D","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI6
Number of Residues4
DetailsSite: {"description":"Involved in metalloproteinase-binding","evidences":[{"source":"PubMed","id":"17196980","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"2E2D","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

Catalytic Information from CSA
site_idCSA1
Number of Residues2
DetailsAnnotated By Reference To The Literature 1hfs
ChainResidueDetails
MMET257
MGLU240

site_idCSA2
Number of Residues1
DetailsAnnotated By Reference To The Literature 1hfs
ChainResidueDetails
MGLU240

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PDB entries from 2025-10-29

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