Structure of PDB 4ase Chain A

Receptor sequence
>4aseA (length=305) Species: 9606 (Homo sapiens) [Search protein sequence]
DPDELPLDEHCERLPYDASKWEFPRDRLKLGKPLGRGAFGQVIEADAFGI
DKTATCRTVAVKMLKEGATHSEHRALMSELKILIHIGHHLNVVNLLGACT
KPGGPLMVIVEFCKFGNLSTYLRSKRNEFVPYYKDFLTLEHLICYSFQVA
KGMEFLASRKCIHRDLAARNILLSEKNVVKICDFGLARDIYKDPDYVRKG
DARLPLKWMAPETIFDRVYTIQSDVWSFGVLLWEIFSLGASPYPGVKIDE
EFCRRLKEGTRMRAPDYTTPEMYQTMLDCWHGEPSQRPTFSELVEHLGNL
LQANA
3D structure
PDB4ase Molecular Conformations, Interactions, and Properties Associated with Drug Efficiency and Clinical Performance Among Vegfr Tk Inhibitors.
ChainA
Resolution1.83 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 D1064
Catalytic site (residue number reindexed from 1) D165 A167 R169 N170 D183 D201
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 AV9 A L840 V848 A866 K868 E885 L889 V916 C919 L1035 C1045 D1046 F1047 N1167 A1168 L34 V42 A60 K62 E79 L83 V110 C113 L172 C182 D183 F184 N304 A305 MOAD: Ki=0.01nM
PDBbind-CN: -logKd/Ki=11.00,Ki=0.01nM
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:4ase, PDBe:4ase, PDBj:4ase
PDBsum4ase
PubMed22988103
UniProtP35968|VGFR2_HUMAN Vascular endothelial growth factor receptor 2 (Gene Name=KDR)

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