Structure of PDB 5i9y Chain A

Receptor sequence
>5i9yA (length=287) Species: 9606 (Homo sapiens) [Search protein sequence]
AVLKFTTEIHPSCVTRQKVIGAGEFGEVYKGMLKTKKEVPVAIKTLKAGY
TEKQRVDFLGEAGIMGQFSHHNIIRLEGVISKYKPMMIITEYMENGALDK
FLREKDGEFSVLQLVGMLRGIAAGMKYLANMNYVHRDLAARNILVNSNLV
CKVSDFGLSRVLEDDPEATYPIRWTAPEAISYRKFTSASDVWSFGIVMWE
VMTYGERPYWELSNHEVMKAINDGFRLPTPMDCPSAIYQLMMQCWQQERA
RRPKFADIVSILDKLIRAPDSLKTLADFDPRVSIRLP
3D structure
PDB5i9y Chemical Proteomics and Structural Biology Define EPHA2 Inhibition by Clinical Kinase Drugs.
ChainA
Resolution1.228 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) D137 A139 R141 N142 D155 D164 P171
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 1N1 A I619 A644 I645 K646 E663 I690 T692 Y694 M695 E696 G698 E706 L746 I20 A42 I43 K44 E61 I88 T90 Y92 M93 E94 G96 E104 L144 MOAD: Kd=2.8nM
PDBbind-CN: -logKd/Ki=8.55,Kd=2.8nM
BindingDB: Kd=0.85nM,IC50=137nM
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:5i9y, PDBe:5i9y, PDBj:5i9y
PDBsum5i9y
PubMed27768280
UniProtP29317|EPHA2_HUMAN Ephrin type-A receptor 2 (Gene Name=EPHA2)

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