Structure of PDB 2qu5 Chain A

Receptor sequence
>2qu5A (length=292) Species: 9606 (Homo sapiens) [Search protein sequence]
HAERLPYDASKWEFPRDRLKLGKPLGRGAFGQVIEADAFGIDKTATCRTV
AVKMLKEGATHSEHRALMSELKILIHIGHHLNVVNLLGACTKPGGPLMVI
TEFCKFGNLSTYLRSKRNEFVPYKVAPEDLYKDFLTLEHLICYSFQVAKG
MEFLASRKCIHRDLAARNILLSEKNVVKICDFGLADARLPLKWMAPETIF
DRVYTIQSDVWSFGVLLWEIFSLGASPYPGVKIDEEFCRRLKEGTRMRAP
DYTTPEMYQTMLDCWHGEPSQRPTFSELVEHLGNLLQANAQQ
3D structure
PDB2qu5 Design, Synthesis, and Evaluation of Orally Active Benzimidazoles and Benzoxazoles as Vascular Endothelial Growth Factor-2 Receptor Tyrosine Kinase Inhibitors.
ChainA
Resolution2.95 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 D1064
Catalytic site (residue number reindexed from 1) D163 A165 R167 N168 D181 D186
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 276 A L840 V848 A866 K868 E885 L889 T916 E917 F918 C919 G922 L1019 L1035 C1045 D1046 F1047 L25 V33 A51 K53 E70 L74 T101 E102 F103 C104 G107 L154 L170 C180 D181 F182 PDBbind-CN: -logKd/Ki=8.06,Ki=8.7nM
BindingDB: Ki=9nM
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:2qu5, PDBe:2qu5, PDBj:2qu5
PDBsum2qu5
PubMed17696416
UniProtP35968|VGFR2_HUMAN Vascular endothelial growth factor receptor 2 (Gene Name=KDR)

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