Structure of PDB 2p2h Chain A

Receptor sequence
>2p2hA (length=292) Species: 9606 (Homo sapiens) [Search protein sequence]
EHAERLPYDASKWEFPRDRLKLGKPLGRQVIEADAFGIDKTATCRTVAVK
MLKEGATHSEHRALMSELKILIHIGHHLNVVNLLGACTKPGGPLMVITEF
CKFGNLSTYLRSKRNEFVPYKVAPEDLYKDFLTLEHLICYSFQVAKGMEF
LASRKCIHRDLAARNILLSEKNVVKICDFGLARLPLKWMAPETIFDRVYT
IQSDVWSFGVLLWEIFSLGASPYPGVKIDEEFCRRLKEGTRMRAPDYTTP
EMYQTMLDCWHGEPSQRPTFSELVEHLGNLLQANAQQDRHHH
3D structure
PDB2p2h Evolution of a Highly Selective and Potent 2-(Pyridin-2-yl)-1,3,5-triazine Tie-2 Kinase Inhibitor
ChainA
Resolution1.95 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
Catalytic site (residue number reindexed from 1) D160 A162 R164 N165 D178
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 994 A V848 A866 K868 E885 T916 F918 C919 G922 L1035 C1045 V30 A48 K50 E67 T98 F100 C101 G104 L167 C177 MOAD: ic50=68nM
PDBbind-CN: -logKd/Ki=7.17,IC50=68nM
BindingDB: IC50=68nM
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
View graph for
Biological Process
External links
PDB RCSB:2p2h, PDBe:2p2h, PDBj:2p2h
PDBsum2p2h
PubMed17253678
UniProtP35968|VGFR2_HUMAN Vascular endothelial growth factor receptor 2 (Gene Name=KDR)

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