Structure of PDB 5ia3 Chain A

Receptor sequence
>5ia3A (length=275) Species: 9606 (Homo sapiens) [Search protein sequence]
LKFTTEIHPSCVTRQKVIGAGEFGEVYKGMLKKKEVPVAIKTLKAGYTEK
QRVDFLGEAGIMGQFSHHNIIRLEGVISKYKPMMIITEYMENGALDKFLR
EKDGEFSVLQLVGMLRGIAAGMKYLANMNYVHRDLAARNILVNSNLVCKV
SDFGLSRIPIRWTAPEAISYRKFTSASDVWSFGIVMWEVMTYGERPYWEL
SNHEVMKAINDGFRLPTPMDCPSAIYQLMMQCWQQERARRPKFADIVSIL
DKLIRAPDSLKTLADFDPRVSIRLP
3D structure
PDB5ia3 Chemical Proteomics and Structural Biology Define EPHA2 Inhibition by Clinical Kinase Drugs.
ChainA
Resolution1.788 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 P780
Catalytic site (residue number reindexed from 1) D134 A136 R138 N139 D152 P159
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 P17 A V627 A644 I645 K646 E663 T692 Y694 M695 G698 L746 V26 A39 I40 K41 E58 T87 Y89 M90 G93 L141 MOAD: Kd=46nM
PDBbind-CN: -logKd/Ki=7.34,Kd=46nM
BindingDB: Kd=3.8nM
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

View graph for
Biological Process
External links
PDB RCSB:5ia3, PDBe:5ia3, PDBj:5ia3
PDBsum5ia3
PubMed27768280
UniProtP29317|EPHA2_HUMAN Ephrin type-A receptor 2 (Gene Name=EPHA2)

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