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5YA5

CRYSTAL STRUCTURE OF c-MET IN COMPLEX WITH NOVEL INHIBITOR

Functional Information from GO Data
ChainGOidnamespacecontents
A0004672molecular_functionprotein kinase activity
A0004713molecular_functionprotein tyrosine kinase activity
A0005524molecular_functionATP binding
A0006468biological_processprotein phosphorylation
Functional Information from PDB Data
site_idAC1
Number of Residues11
Detailsbinding site for residue 6TD A 1401
ChainResidue
AALA1108
AALA1226
ATYR1230
ATYR1159
AMET1160
AASP1164
AASN1167
AARG1208
AMET1211
AALA1221
AASP1222

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 Residues1
DetailsACT_SITE: Proton acceptor => ECO:0000255|PROSITE-ProRule:PRU00159, ECO:0000255|PROSITE-ProRule:PRU10028
ChainResidueDetails
AASP1204

site_idSWS_FT_FI2
Number of Residues1
DetailsBINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU00159
ChainResidueDetails
AILE1084

site_idSWS_FT_FI3
Number of Residues1
DetailsBINDING:
ChainResidueDetails
ALYS1110

site_idSWS_FT_FI4
Number of Residues1
DetailsMOD_RES: Phosphotyrosine => ECO:0000269|PubMed:12475979
ChainResidueDetails
ATYR1230

site_idSWS_FT_FI5
Number of Residues1
DetailsMOD_RES: Phosphotyrosine; by autocatalysis => ECO:0000269|PubMed:12475979
ChainResidueDetails
ATYR1234

site_idSWS_FT_FI6
Number of Residues1
DetailsMOD_RES: Phosphotyrosine; by autocatalysis => ECO:0000269|PubMed:12475979, ECO:0000269|PubMed:1655790
ChainResidueDetails
ATYR1235

site_idSWS_FT_FI7
Number of Residues1
DetailsMOD_RES: Phosphothreonine => ECO:0007744|PubMed:19369195
ChainResidueDetails
ATHR1289

218853

PDB entries from 2024-04-24

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