Structure of PDB 3vid Chain A

Receptor sequence
>3vidA (length=299) Species: 9606 (Homo sapiens) [Search protein sequence]
LDEHCERLPYDASKWEFPRDRLKLGKPLGRGAFGQVIEADAFGIDKTATC
RTVAVKMLKEGATHSEHRALMSELKILIHIGHHLNVVNLLGACTKPGGPL
MVIVEFCKFGNLSTYLRSKRNEFVPYKEAPEDLYKDFLTLEHLICYSFQV
AKGMEFLASRKCIHRDLAARNILLSEKNVVKICDYKDPDYVRKGDARLPL
KWMAPETIFDRVYTIQSDVWSFGVLLWEIFSLGASPYPGVKIDEEFCRRL
KEGTRMRAPDYTTPEMYQTMLDCWHGEPSQRPTFSELVEHLGNLLQANA
3D structure
PDB3vid A Back-to-Front Fragment-Based Drug Design Search Strategy Targeting the DFG-Out Pocket of Protein Tyrosine Kinases.
ChainA
Resolution2.3 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) D166 R170 N171 D184 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 4TT A V848 A866 E917 F918 C919 G922 L1035 V36 A54 E105 F106 C107 G110 L173 PDBbind-CN: -logKd/Ki=6.21,IC50=620nM
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

View graph for
Biological Process
External links
PDB RCSB:3vid, PDBe:3vid, PDBj:3vid
PDBsum3vid
PubMed24900475
UniProtP35968|VGFR2_HUMAN Vascular endothelial growth factor receptor 2 (Gene Name=KDR)

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