Structure of PDB 2rl5 Chain A

Receptor sequence
>2rl5A (length=294) Species: 9606 (Homo sapiens) [Search protein sequence]
EHAERLPYDASKWEFPRDRLKLGKPLGRGQVIEADAFGIDKTATCRTVAV
KMLKEGATHSEHRALMSELKILIHIGHHLNVVNLLGACTKPGGPLMVITE
FCKFGNLSTYLRSKRNEFVPYKVAPEDLYKDFLTLEHLICYSFQVAKGME
FLASRKCIHRDLAARNILLSEKNVVKICDFGLDARLPLKWMAPETIFDRV
YTIQSDVWSFGVLLWEIFSLGASPYPGVKIDEEFCRRLKEGTRMRAPDYT
TPEMYQTMLDCWHGEPSQRPTFSELVEHLGNLLQANAQQDRHHH
3D structure
PDB2rl5 Novel 2,3-dihydro-1,4-benzoxazines as potent and orally bioavailable inhibitors of tumor-driven angiogenesis.
ChainA
Resolution2.65 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) D161 A163 R165 N166 D179 D183
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 2RL A L840 V848 A866 E885 L889 T916 F918 C919 L1019 L1035 C1045 D1046 F1047 L26 V31 A49 E68 L72 T99 F101 C102 L152 L168 C178 D179 F180 PDBbind-CN: -logKd/Ki=8.40,IC50=4nM
BindingDB: IC50=0.5nM
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:2rl5, PDBe:2rl5, PDBj:2rl5
PDBsum2rl5
PubMed18311900
UniProtP35968|VGFR2_HUMAN Vascular endothelial growth factor receptor 2 (Gene Name=KDR)

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