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3QTI

c-Met Kinase in Complex with NVP-BVU972

Functional Information from GO Data
ChainGOidnamespacecontents
A0004672molecular_functionprotein kinase activity
A0004713molecular_functionprotein tyrosine kinase activity
A0005524molecular_functionATP binding
A0006468biological_processprotein phosphorylation
B0004672molecular_functionprotein kinase activity
B0004713molecular_functionprotein tyrosine kinase activity
B0005524molecular_functionATP binding
B0006468biological_processprotein phosphorylation
Functional Information from PDB Data
site_idAC1
Number of Residues12
DetailsBINDING SITE FOR RESIDUE 3QT A 1
ChainResidue
AILE1084
AASP1222
AALA1226
ATYR1230
AALA1108
ALEU1140
APRO1158
AMET1160
AASP1164
AARG1208
AMET1211
AALA1221

site_idAC2
Number of Residues5
DetailsBINDING SITE FOR RESIDUE CL A 1361
ChainResidue
AHOH53
ALYS1179
AGLY1346
AGLU1347
AHIS1348

site_idAC3
Number of Residues12
DetailsBINDING SITE FOR RESIDUE 3QT B 1
ChainResidue
BILE1084
BALA1108
BLEU1140
BPRO1158
BMET1160
BASP1164
BARG1208
BMET1211
BALA1221
BASP1222
BALA1226
BTYR1230

site_idAC4
Number of Residues5
DetailsBINDING SITE FOR RESIDUE CL B 2
ChainResidue
BHOH55
BLYS1179
BGLY1346
BGLU1347
BHIS1348

site_idAC5
Number of Residues7
DetailsBINDING SITE FOR RESIDUE GOL B 3
ChainResidue
BHOH55
BHOH82
BHOH215
BTHR1343
BPHE1344
BGLU1347
BHIS1348

Functional Information from PROSITE/UniProt
site_idPS00107
Number of Residues27
DetailsPROTEIN_KINASE_ATP Protein kinases ATP-binding region signature. IGRGHFGCVYhGtlldndgkkih.......CAVK
ChainResidueDetails
AILE1084-LYS1110

site_idPS00109
Number of Residues13
DetailsPROTEIN_KINASE_TYR Tyrosine protein kinases specific active-site signature. FVHrDLAARNCML
ChainResidueDetails
APHE1200-LEU1212

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsACT_SITE: Proton acceptor => ECO:0000255|PROSITE-ProRule:PRU00159, ECO:0000255|PROSITE-ProRule:PRU10028
ChainResidueDetails
AASP1204
BASP1204

site_idSWS_FT_FI2
Number of Residues2
DetailsBINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU00159
ChainResidueDetails
AILE1084
BILE1084

site_idSWS_FT_FI3
Number of Residues2
DetailsBINDING:
ChainResidueDetails
ALYS1110
BLYS1110

site_idSWS_FT_FI4
Number of Residues2
DetailsMOD_RES: Phosphotyrosine => ECO:0000269|PubMed:12475979
ChainResidueDetails
ATYR1230
BTYR1230

site_idSWS_FT_FI5
Number of Residues2
DetailsMOD_RES: Phosphotyrosine; by autocatalysis => ECO:0000269|PubMed:12475979
ChainResidueDetails
APHE1234
BPHE1234

site_idSWS_FT_FI6
Number of Residues2
DetailsMOD_RES: Phosphotyrosine; by autocatalysis => ECO:0000269|PubMed:12475979, ECO:0000269|PubMed:1655790
ChainResidueDetails
AASP1235
BASP1235

site_idSWS_FT_FI7
Number of Residues2
DetailsMOD_RES: Phosphothreonine => ECO:0007744|PubMed:19369195
ChainResidueDetails
ATHR1289
BTHR1289

site_idSWS_FT_FI8
Number of Residues2
DetailsMOD_RES: Phosphotyrosine; by autocatalysis => ECO:0000269|PubMed:12475979, ECO:0000269|PubMed:7513258
ChainResidueDetails
ATYR1349
BTYR1349

site_idSWS_FT_FI9
Number of Residues2
DetailsMOD_RES: Phosphotyrosine; by autocatalysis => ECO:0000269|PubMed:15735664, ECO:0000269|PubMed:7513258
ChainResidueDetails
ATYR1356
BTYR1356

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PDB entries from 2024-07-24

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