Structure of PDB 1ywn Chain A

Receptor sequence
>1ywnA (length=281) Species: 9606 (Homo sapiens) [Search protein sequence]
LPYDASKWEFPRDRLKLGKPLGRGAFGQVIEADAFGIDKTATCRTVAVKM
LTHSEHRALMSELKILIHIGHHLNVVNLLGACTKPGGPLMVIVEFCKFGN
LSTYLRSKRNEFVPFLTLEHLICYSFQVAKGMEFLASRKCIHRDLAARNI
LLSEKNVVKICDIYKDPDYVRKGDARLPLKWMAPETIFDRVYTIQSDVWS
FGVLLWEIFSLGASPYPGVKIDEEFCRRLKEGTRMRAPDYTTPEMYQTML
DCWHGEPSQRPTFSELVEHLGNLLQANAQQD
3D structure
PDB1ywn Novel 4-amino-furo[2,3-d]pyrimidines as Tie-2 and VEGFR2 dual inhibitors
ChainA
Resolution1.71 Å
3D
structure
Catalytic site residues are labeled in the structure
[Spin on]
[Spin off]
[Reset orientation]

[High quality]
[Low quality]

[White background]
[Black background]

[Download]
[Download structure with residue number starting from 1]
Enzymatic activity
Catalytic site (original residue number in PDB) D1026 A1028 R1030 N1031 D1044 K1053 D1062
Catalytic site (residue number reindexed from 1) D144 A146 R148 N149 D162 K165 D174
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 LIF A L838 G841 V846 E883 V897 F916 C917 L1033 C1043 D1044 L21 G24 V29 E62 V76 F95 C96 L151 C161 D162 MOAD: ic50~0.003uM
BindingDB: IC50=3nM
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

View graph for
Molecular Function
View graph for
Biological Process
External links
PDB RCSB:1ywn, PDBe:1ywn, PDBj:1ywn
PDBsum1ywn
PubMed15837294
UniProtP35968|VGFR2_HUMAN Vascular endothelial growth factor receptor 2 (Gene Name=KDR)

[Back to BioLiP]