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2RFN

x-ray structure of c-Met with 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 Residues18
DetailsBINDING SITE FOR RESIDUE AM7 A 1
ChainResidue
AILE1084
ALEU1140
ALEU1142
ALEU1157
APRO1158
ATYR1159
AMET1160
ALYS1161
AGLY1163
AMET1211
APHE1089
AVAL1092
AALA1108
ALYS1110
APHE1124
AGLU1127
AGLY1128
AMET1131

site_idAC2
Number of Residues17
DetailsBINDING SITE FOR RESIDUE AM7 B 1
ChainResidue
BILE1084
BPHE1089
BVAL1092
BALA1108
BLYS1110
BPHE1124
BGLU1127
BMET1131
BLEU1142
BILE1145
BLEU1157
BPRO1158
BTYR1159
BMET1160
BLYS1161
BGLY1163
BMET1211

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

Catalytic Information from CSA
site_idCSA1
Number of Residues2
DetailsAnnotated By Reference To The Literature 1ir3
ChainResidueDetails
AASP1204
AARG1208

site_idCSA2
Number of Residues2
DetailsAnnotated By Reference To The Literature 1ir3
ChainResidueDetails
BASP1204
BARG1208

site_idCSA3
Number of Residues2
DetailsAnnotated By Reference To The Literature 1ir3
ChainResidueDetails
AALA1206
AASP1204

site_idCSA4
Number of Residues2
DetailsAnnotated By Reference To The Literature 1ir3
ChainResidueDetails
BALA1206
BASP1204

site_idCSA5
Number of Residues3
DetailsAnnotated By Reference To The Literature 1ir3
ChainResidueDetails
AASN1209
AALA1206
AASP1204

site_idCSA6
Number of Residues3
DetailsAnnotated By Reference To The Literature 1ir3
ChainResidueDetails
BASN1209
BALA1206
BASP1204

219140

PDB entries from 2024-05-01

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