Structure of PDB 2qu6 Chain B

Receptor sequence
>2qu6B (length=260) Species: 9606 (Homo sapiens) [Search protein sequence]
YDASKWEFPRDRLKLGKPLGRQVIEADAFGIDKTATCRTVAVKMLKEGAT
HSEHRALMSELKILIHIGHHLNVVNLLGACTKPGGPLMVITEFCKFGNLS
TYLRSKRNEFVPFLTLEHLICYSFQVAKGMEFLASRKCIHRDLAARNILL
SEKNVVKICDFLPLKWMAPETIFDRVYTIQSDVWSFGVLLWEIFSLGASP
YPGVKIDEEFCRRLKEGTRMRAPDYTTPEMYQTMLDCWHGEPSQRPTFSE
LVEHLGNLLQ
3D structure
PDB2qu6 Design, Synthesis, and Evaluation of Orally Active Benzimidazoles and Benzoxazoles as Vascular Endothelial Growth Factor-2 Receptor Tyrosine Kinase Inhibitors.
ChainB
Resolution2.1 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) D142 A144 R146 N147 D160
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 857 B V848 A866 E885 T916 E917 F918 C919 I1025 R1027 L1035 C1045 D1046 F1047 V23 A41 E60 T91 E92 F93 C94 I139 R141 L149 C159 D160 F161 MOAD: Ki=3nM
BindingDB: IC50=4.6nM,Ki=2.8nM
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:2qu6, PDBe:2qu6, PDBj:2qu6
PDBsum2qu6
PubMed17696416
UniProtP35968|VGFR2_HUMAN Vascular endothelial growth factor receptor 2 (Gene Name=KDR)

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