Structure of PDB 5nk3 Chain A

Receptor sequence
>5nk3A (length=281) Species: 9606 (Homo sapiens) [Search protein sequence]
VLKFTTEIHPSCVTRQKVIGAGEFGEVYKGMLKTKEVPVAIKTLKAGYTE
KQRVDFLGEAGIMGQFSHHNIIRLEGVISKYKPMMIITEYMENGALDKFL
REKDGEFSVLQLVGMLRGIAAGMKYLANMNYVHRDLAARNILVNSNLVCK
VSDFGLSRVLEDDPEATYTGKIPIRWTAPEAISYRKFTSASDVWSFGIVM
WEVMTYGERPYWELSNHEVMKAINDGFRLPTPMDCPSAIYQLMMQCWQQE
RARRPKFADIVSILDKLIRAPDSLKTLADFD
3D structure
PDB5nk3 Chemoproteomics-Aided Medicinal Chemistry for the Discovery of EPHA2 Inhibitors.
ChainA
Resolution1.586 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 D766 P780
Catalytic site (residue number reindexed from 1) D135 A137 R139 N140 D153 D162 P173
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 92Q A I619 A644 I645 K646 M667 I690 T692 Y694 M695 G698 A699 L746 I19 A40 I41 K42 M63 I86 T88 Y90 M91 G94 A95 L142 MOAD: Kd=38.02nM
PDBbind-CN: -logKd/Ki=7.42,Kd=38nM
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:5nk3, PDBe:5nk3, PDBj:5nk3
PDBsum5nk3
PubMed28544567
UniProtP29317|EPHA2_HUMAN Ephrin type-A receptor 2 (Gene Name=EPHA2)

[Back to BioLiP]