Structure of PDB 5ia4 Chain A

Receptor sequence
>5ia4A (length=269) Species: 9606 (Homo sapiens) [Search protein sequence]
TTEIHPSCVTRQKVIGAGEFGEVYKGMLKKKEVPVAIKTLKAGYTEKQRV
DFLGEAGIMGQFSHHNIIRLEGVISKYKPMMIITEYMENGALDKFLREKD
GEFSVLQLVGMLRGIAAGMKYLANMNYVHRDLAARNILVNSNLVCKVSDF
GLSRVLEDDPEATYTTSGGKIPIRWTAPEAISYRKFTSASDVWSFGIVMW
EVMTYGERPYWELSNHEVMKAINDGFRLPTPMDCPSAIYQLMMQCWQQER
ARRPKFADIVSILDKLIRA
3D structure
PDB5ia4 Chemical Proteomics and Structural Biology Define EPHA2 Inhibition by Clinical Kinase Drugs.
ChainA
Resolution1.797 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 P172
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 88Z A I619 A644 K646 E663 M667 Y694 M695 E696 L730 L746 S756 D757 F758 I15 A36 K38 E55 M59 Y86 M87 E88 L122 L138 S148 D149 F150 MOAD: Kd=52nM
PDBbind-CN: -logKd/Ki=7.28,Kd=52nM
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:5ia4, PDBe:5ia4, PDBj:5ia4
PDBsum5ia4
PubMed27768280
UniProtP29317|EPHA2_HUMAN Ephrin type-A receptor 2 (Gene Name=EPHA2)

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