Structure of PDB 5ew3 Chain A

Receptor sequence
>5ew3A (length=274) Species: 9606 (Homo sapiens) [Search protein sequence]
PYDASKWEFPRDRLKLGKPLGRGAFGQVIEADAFGIDKTATCRTVAVKML
KEGATHSEHRALMSELKILIHIGHHLNVVNLLGACTKPGGPLMVIVEFCK
FGNLSTYLRSKRNEFVPYKVKDFLTLEHLICYSFQVAKGMEFLASRKCIH
RDLAARNILLSEKNVVKICDFGLPLKWMAPETIFDRVYTIQSDVWSFGVL
LWEIFSLGASPYPGVKIDEEFCRRLKEGTRMRAPDYTTPEMYQTMLDCWH
GEPSQRPTFSELVEHLGNLLQANA
3D structure
PDB5ew3 A Novel Potent Oral Series of VEGFR2 Inhibitors Abrogate Tumor Growth by Inhibiting Angiogenesis.
ChainA
Resolution2.5 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) D152 A154 R156 N157 D170
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 5T2 A A866 K868 E885 V916 C919 H1026 L1035 I1044 C1045 D1046 F1047 A46 K48 E65 V96 C99 H150 L159 I168 C169 D170 F171 MOAD: ic50=0.0012uM
PDBbind-CN: -logKd/Ki=8.92,IC50=0.0012uM
BindingDB: IC50=23nM
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:5ew3, PDBe:5ew3, PDBj:5ew3
PDBsum5ew3
PubMed26629594
UniProtP35968|VGFR2_HUMAN Vascular endothelial growth factor receptor 2 (Gene Name=KDR)

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