Structure of PDB 3cpc Chain A

Receptor sequence
>3cpcA (length=284) Species: 9606 (Homo sapiens) [Search protein sequence]
LPYDASKWEFPRDRLKLGKPLQVIEADAFGIDKTATCRTVAVKMLKEGAT
HSEHRALMSELKILIHIGHHLNVVNLLGACTKPGGPLMVITEFCKFGNLS
TYLRSKRNEFVPYKVAPEDLYKDFLTLEHLICYSFQVAKGMEFLASRKCI
HRDLAARNILLSEKNVVKICDFLPLKWMAPETIFDRVYTIQSDVWSFGVL
LWEIFSLGASPYPGVKIDEEFCRRLKEGTRMRAPDYTTPEMYQTMLDCWH
GEPSQRPTFSELVEHLGNLLQANAQQDRHHHHHH
3D structure
PDB3cpc Discovery of Aryl Aminoquinazoline Pyridones as Potent, Selective, and Orally Efficacious Inhibitors of Receptor Tyrosine Kinase c-Kit.
ChainA
Resolution2.4 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) D1028 A1030 R1032 N1033 D1046
Catalytic site (residue number reindexed from 1) D153 A155 R157 N158 D171
Enzyme Commision number 2.7.10.1: receptor protein-tyrosine kinase.
Interaction with ligand
Site
#		 Ligand Ligand
chain		 Binding residues on receptor
(original residue number in PDB)		 Binding residues on receptor
(residue number reindexed from 1)		 Binding affinity
BS01 C52 A V848 A866 K868 E885 L889 V899 T916 C919 L1035 C1045 D1046 F1047 V23 A41 K43 E60 L64 V74 T91 C94 L160 C170 D171 F172 PDBbind-CN: -logKd/Ki=5.30,IC50=5uM
BindingDB: IC50=>5000nM
Gene Ontology
Molecular Function
GO:0004672 protein kinase activity
GO:0004713 protein tyrosine kinase activity
GO:0004714 transmembrane receptor protein tyrosine kinase activity
GO:0005524 ATP binding
Biological Process
GO:0006468 protein phosphorylation
GO:0007169 cell surface receptor protein tyrosine kinase signaling pathway

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Molecular Function
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Biological Process
External links
PDB RCSB:3cpc, PDBe:3cpc, PDBj:3cpc
PDBsum3cpc
PubMed18447379
UniProtP35968|VGFR2_HUMAN Vascular endothelial growth factor receptor 2 (Gene Name=KDR)

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