Structure of PDB 5nk2 Chain A

Receptor sequence
>5nk2A (length=290) Species: 9606 (Homo sapiens) [Search protein sequence]
NQAVLKFTTEIHPSCVTRQKVIGAGEFGEVYKGMLKKEVPVAIKTLKAGY
TEKQRVDFLGEAGIMGQFSHHNIIRLEGVISKYKPMMIITEYMENGALDK
FLREKDGEFSVLQLVGMLRGIAAGMKYLANMNYVHRDLAARNILVNSNLV
CKVSDFGLSRVLEDDPEATYGKIPIRWTAPEAISYRKFTSASDVWSFGIV
MWEVMTYGERPYWELSNHEVMKAINDGFRLPTPMDCPSAIYQLMMQCWQQ
ERARRPKFADIVSILDKLIRAPDSLKTLADFDPRVSIRLP
3D structure
PDB5nk2 Chemoproteomics-Aided Medicinal Chemistry for the Discovery of EPHA2 Inhibitors.
ChainA
Resolution1.649 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) D137 A139 R141 N142 D155 D164 P174
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 8ZZ A I619 A644 I645 K646 E663 I690 T692 M695 G698 L746 I22 A42 I43 K44 E61 I88 T90 M93 G96 L144 MOAD: Kd=0.182uM
PDBbind-CN: -logKd/Ki=6.74,Kd=182nM
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:5nk2, PDBe:5nk2, PDBj:5nk2
PDBsum5nk2
PubMed28544567
UniProtP29317|EPHA2_HUMAN Ephrin type-A receptor 2 (Gene Name=EPHA2)

[Back to BioLiP]