Structure of PDB 3be2 Chain A

Receptor sequence
>3be2A (length=290) Species: 9606 (Homo sapiens) [Search protein sequence]
EHAERLPYDASKWEFPRDRLKLGKPLGRGAFGQVIEADAFGIDTCRTVAV
KMLKEGATHSEHRALMSELKILIHIGHHLNVVNLLGACTKPGGPLMVITE
FCKFGNLSTYLRSKRNEFVPYKVAPEDLYKDFLTLEHLICYSFQVAKGME
FLASRKCIHRDLAARNILLSEKNVVKICDFGPLKWMAPETIFDRVYTIQS
DVWSFGVLLWEIFSLGASPYPGVKIDEEFCRRLKEGTRMRAPDYTTPEMY
QTMLDCWHGEPSQRPTFSELVEHLGNLLQANAQQDRHHHH
3D structure
PDB3be2 Naphthamides as novel and potent vascular endothelial growth factor receptor tyrosine kinase inhibitors: design, synthesis, and evaluation.
ChainA
Resolution1.75 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) D161 A163 R165 N166 D179
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 RAJ A V848 A866 E885 T916 F918 C919 H1026 L1035 I1044 C1045 D1046 F1047 V34 A49 E68 T99 F101 C102 H159 L168 I177 C178 D179 F180 MOAD: ic50=2nM
PDBbind-CN: -logKd/Ki=8.70,IC50=2nM
BindingDB: IC50=2nM
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:3be2, PDBe:3be2, PDBj:3be2
PDBsum3be2
PubMed18324761
UniProtP35968|VGFR2_HUMAN Vascular endothelial growth factor receptor 2 (Gene Name=KDR)

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