Structure of PDB 1y6b Chain A

Receptor sequence
>1y6bA (length=266) Species: 9606 (Homo sapiens) [Search protein sequence]
RLPYDASKWEFPRDRLKLGKPLGRGGQVIEADAFGIDKTATCRTVAVKML
KATHSEHRALMSELKILIHIGHHLNVVNLLGACTKPGGPLMVIVEFCKFG
NLSTYLRSKRNEFVPYFLTLEHLICYSFQVAKGMEFLASRKCIHRDLAAR
NILLSEKNVVKICDFPLKWMAPETIFDRVYTIQSDVWSFGVLLWEIFSLG
ASPYPGVKIDEEFCRRLKEGTRMRAPDYTTPEMYQTMLDCWHGEPSQRPT
FSELVEHLGNLLQANA
3D structure
PDB1y6b Discovery and evaluation of 2-anilino-5-aryloxazoles as a novel class of VEGFR2 kinase inhibitors.
ChainA
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) D1026 R1030 N1031 D1044
Catalytic site (residue number reindexed from 1) D146 R150 N151 D164
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 AAX A L838 V846 A864 K866 E883 V912 V914 F916 C917 G920 N921 L1033 F1045 L22 V28 A46 K48 E63 V92 V94 F96 C97 G100 N101 L153 F165 MOAD: ic50=38nM
PDBbind-CN: -logKd/Ki=7.42,IC50=38nM
BindingDB: IC50=38nM
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:1y6b, PDBe:1y6b, PDBj:1y6b
PDBsum1y6b
PubMed15743202
UniProtP35968|VGFR2_HUMAN Vascular endothelial growth factor receptor 2 (Gene Name=KDR)

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