Structure of PDB 5ia0 Chain A

Receptor sequence
>5ia0A (length=263) Species: 9606 (Homo sapiens) [Search protein sequence]
FTTEIHPSCVTRQKVIGAGEFGEVYKGMLKTKEVPVAIKTLKAGYTEKQR
VDFLGEAGIMGQFSHHNIIRLEGVISKYKPMMIITEYMENGALDKFLREK
DGEFSVLQLVGMLRGIAAGMKYLANMNYVHRDLAARNILVNSNLVCKVSD
FGIPIRWTAPEAISYRKFTSASDVWSFGIVMWEVMTYGERPYWELSNHEV
MKAINDGFRLPTPMDCPSAIYQLMMQCWQQERARRPKFADIVSILDKLIR
APDSLKTLADFDP
3D structure
PDB5ia0 Chemical Proteomics and Structural Biology Define EPHA2 Inhibition by Clinical Kinase Drugs.
ChainA
Resolution1.948 Å
3D
structure
Catalytic site residues are labeled in the structure
[Spin on]
[Spin off]
[Reset orientation]

[High quality]
[Low quality]

[White background]
[Black background]

[Download]
[Download structure with residue number starting from 1]
Enzymatic activity
Catalytic site (original residue number in PDB) D739 A741 R743 N744 D757 P780
Catalytic site (residue number reindexed from 1) D132 A134 R136 N137 D150 P154
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 A5B A I619 A621 V627 A644 K646 Y694 M695 E696 G698 K702 L746 I16 A18 V24 A37 K39 Y87 M88 E89 G91 K95 L139 MOAD: Kd=187nM
PDBbind-CN: -logKd/Ki=6.73,Kd=187nM
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

View graph for
Molecular Function
View graph for
Biological Process
External links
PDB RCSB:5ia0, PDBe:5ia0, PDBj:5ia0
PDBsum5ia0
PubMed27768280
UniProtP29317|EPHA2_HUMAN Ephrin type-A receptor 2 (Gene Name=EPHA2)

[Back to BioLiP]