Structure of PDB 5ia2 Chain A

Receptor sequence
>5ia2A (length=287) Species: 9606 (Homo sapiens) [Search protein sequence]
NQAVLKFTTEIHPSCVTRQKVIGAGEFGEVYKGMLKTKEVPVAIKTLKAG
YTEKQRVDFLGEAGIMGQFSHHNIIRLEGVISKYKPMMIITEYMENGALD
KFLREKDGEFSVLQLVGMLRGIAAGMKYLANMNYVHRDLAARNILVNSNL
VCKVSDFGLSRVLEDDPEATYTTSGGKIPIRWTAPEAISYRKFTSASDVW
SFGIVMWEVMTYGERPYWELSNHEVMKAINDGFRLPTPMDCPSAIYQLMM
QCWQQERARRPKFADIVSILDKLIRAPDSLKTLADFD
3D structure
PDB5ia2 Chemical Proteomics and Structural Biology Define EPHA2 Inhibition by Clinical Kinase Drugs.
ChainA
Resolution1.619 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) D138 A140 R142 N143 D156 D165 P179
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 L66 A I619 V627 A644 E663 T692 Y694 M695 G698 L746 D757 I22 V30 A43 E62 T91 Y93 M94 G97 L145 D156 MOAD: Kd=19nM
PDBbind-CN: -logKd/Ki=7.72,Kd=19nM
BindingDB: IC50=2.3nM
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:5ia2, PDBe:5ia2, PDBj:5ia2
PDBsum5ia2
PubMed27768280
UniProtP29317|EPHA2_HUMAN Ephrin type-A receptor 2 (Gene Name=EPHA2)

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