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3RHK

Crystal structure of the catalytic domain of c-Met kinase in complex with ARQ 197

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 Residues14
DetailsBINDING SITE FOR RESIDUE M97 A 1
ChainResidue
AHOH164
APRO1158
ATYR1159
AMET1160
AGLY1163
APHE1223
AILE1084
AGLY1085
APHE1089
AVAL1092
AALA1108
ALYS1110
ALEU1140
ALEU1157

site_idAC2
Number of Residues13
DetailsBINDING SITE FOR RESIDUE M97 B 1
ChainResidue
BILE1084
BGLY1085
BPHE1089
BALA1108
BLYS1110
BLEU1140
BLEU1157
BPRO1158
BTYR1159
BMET1160
BGLY1163
BMET1211
BPHE1223

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

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PDB entries from 2024-10-09

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