Structure of PDB 6jok Chain A

Receptor sequence
>6jokA (length=338) Species: 9606 (Homo sapiens) [Search protein sequence]
EIRWRVIESISPDGHEYIYVDPMQLPYDSRWEFPRDGLVLGRVLGSGAFG
KVVEGTAYGLSRSQPVMKVAVKMLKPTARSSEKQALMSELKIMTHLGPHL
NIVNLLGACTKSGPIYIITEYCFYGDLVNYLHKNRDSFLSHEVKNLLSDD
NSEGLTLLDLLSFTYQVARGMEFLASKNCVHRDLAARNVLLAQGKIVKIC
DFGLARDIMHDSNYVSKGSTFLPVKWMAPESIFDNLYTTLSDVWSYGILL
WEIFSLGGTPYPGMMVDSTFYNKIKSGYRMAKPDHATSEVYEIMVKCWNS
EPEKRPSFYHLSEIVENLLPGQYKKSYEKIHLDFLKSD
3D structure
PDB6jok Crystal structure of PDGFRA in complex with sunitinib by soaking
ChainA
Resolution3.8 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) D818 R822 N823 D836
Catalytic site (residue number reindexed from 1) D183 R187 N188 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 B49 A L599 V607 A625 K627 V658 T674 E675 C677 F678 G680 N684 L825 L44 V52 A70 K72 V103 T119 E120 C122 F123 G125 N129 L190 BindingDB: Kd=0.790000nM,IC50=130nM
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:6jok, PDBe:6jok, PDBj:6jok
PDBsum6jok
PubMed
UniProtP16234|PGFRA_HUMAN Platelet-derived growth factor receptor alpha (Gene Name=PDGFRA)

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