Structure of PDB 5i9x Chain A

Receptor sequence
>5i9xA (length=284) Species: 9606 (Homo sapiens) [Search protein sequence]
FTTEIHPSCVTRQKVIGAGEFGEVYKGMLKTEVPVAIKTLKAGYTEKQRV
DFLGEAGIMGQFSHHNIIRLEGVISKYKPMMIITEYMENGALDKFLREKD
GEFSVLQLVGMLRGIAAGMKYLANMNYVHRDLAARNILVNSNLVCKVSDF
GLSRVLEDDPEATYGKIPIRWTAPEAISYRKFTSASDVWSFGIVMWEVMT
YGERPYWELSNHEVMKAINDGFRLPTPMDCPSAIYQLMMQCWQQERARRP
KFADIVSILDKLIRAPDSLKTLADFDPRVSIRLP
3D structure
PDB5i9x Chemical Proteomics and Structural Biology Define EPHA2 Inhibition by Clinical Kinase Drugs.
ChainA
Resolution1.427 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) D739 A741 R743 N744 D757 D766 P780
Catalytic site (residue number reindexed from 1) D131 A133 R135 N136 D149 D158 P168
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 DB8 A I619 A644 I645 K646 E663 I690 T692 Y694 M695 G698 L746 I16 A36 I37 K38 E55 I82 T84 Y86 M87 G90 L138 MOAD: Kd=30nM
PDBbind-CN: -logKd/Ki=7.52,Kd=30nM
BindingDB: Kd=18nM
Gene Ontology
Molecular Function
GO:0004672 protein kinase activity
GO:0004713 protein tyrosine kinase activity
GO:0005524 ATP binding
Biological Process
GO:0006468 protein phosphorylation

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Molecular Function
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Biological Process
External links
PDB RCSB:5i9x, PDBe:5i9x, PDBj:5i9x
PDBsum5i9x
PubMed27768280
UniProtP29317|EPHA2_HUMAN Ephrin type-A receptor 2 (Gene Name=EPHA2)

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