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3F66

Human c-Met Kinase in complex with quinoxaline inhibitor

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 Residues10
DetailsBINDING SITE FOR RESIDUE IHX A 1
ChainResidue
AGBL3
AMET1211
AHOH336
AILE1084
AALA1108
ALEU1140
ALEU1157
APRO1158
ATYR1159
AMET1160

site_idAC2
Number of Residues5
DetailsBINDING SITE FOR RESIDUE GBL A 3
ChainResidue
AIHX1
AARG1208
AALA1221
AASP1222
ATYR1230

site_idAC3
Number of Residues6
DetailsBINDING SITE FOR RESIDUE GBL A 4
ChainResidue
AMET1131
ALEU1140
ALEU1142
APHE1223
AGLY1224
ALEU1225

site_idAC4
Number of Residues5
DetailsBINDING SITE FOR RESIDUE GBL A 5
ChainResidue
AHOH339
APHE1168
APRO1176
AASP1180
APHE1184

site_idAC5
Number of Residues10
DetailsBINDING SITE FOR RESIDUE IHX B 2
ChainResidue
BGBL1
BHOH342
BILE1084
BALA1108
BLEU1157
BPRO1158
BTYR1159
BMET1160
BLYS1161
BMET1211

site_idAC6
Number of Residues5
DetailsBINDING SITE FOR RESIDUE GBL B 1
ChainResidue
BIHX2
BARG1208
BALA1221
BASP1222
BTYR1230

site_idAC7
Number of Residues6
DetailsBINDING SITE FOR RESIDUE GBL B1350
ChainResidue
BASP1180
BGLY1183
BPHE1184
BGLN1187
BPHE1341
BTYR1349

site_idAC8
Number of Residues6
DetailsBINDING SITE FOR RESIDUE NA B 6
ChainResidue
BHOH155
BHOH201
BHOH280
BHOH289
BLYS1132
BPHE1134

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
ATYR1234
BTYR1234

site_idSWS_FT_FI6
Number of Residues2
DetailsMOD_RES: Phosphotyrosine; by autocatalysis => ECO:0000269|PubMed:12475979, ECO:0000269|PubMed:1655790
ChainResidueDetails
ATYR1235
BTYR1235

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

218853

PDB entries from 2024-04-24

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