Structure of PDB 3vhk Chain A

Receptor sequence
>3vhkA (length=297) Species: 9606 (Homo sapiens) [Search protein sequence]
DEHCERLPYDASKWEFPRDRLKLGKPLGRGAFGQVIEADAFGIDKTATCR
TVAVKMLKEGATHSEHRALMSELKILIHIGHHLNVVNLLGACTKPGGPLM
VIVEFCKFGNLSTYLRSKRNEFVPYKYKDFLTLEHLICYSFQVAKGMEFL
ASRKCIHRDLAARNILLSEKNVVKICDFGLARDIYKDPDYVRKARLPLKW
MAPETIFDRVYTIQSDVWSFGVLLWEIFSLGASPYPGVKIDEEFCRRLKE
GTRMRAPDYTTPEMYQTMLDCWHGEPSQRPTFSELVEHLGNLLQANA
3D structure
PDB3vhk A Back-to-Front Fragment-Based Drug Design Search Strategy Targeting the DFG-Out Pocket of Protein Tyrosine Kinases.
ChainA
Resolution2.49 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 R1032 N1033 D1046 K1055
Catalytic site (residue number reindexed from 1) D159 R163 N164 D177 K186
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 BPK A V848 K868 E885 L1019 C1045 D1046 F1047 V35 K55 E72 L150 C176 D177 F178 PDBbind-CN: -logKd/Ki=4.60,Ki=25uM
BindingDB: Ki=25000nM,IC50=100000nM
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:3vhk, PDBe:3vhk, PDBj:3vhk
PDBsum3vhk
PubMed24900475
UniProtP35968|VGFR2_HUMAN Vascular endothelial growth factor receptor 2 (Gene Name=KDR)

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