Structure of PDB 5nk4 Chain A

Receptor sequence
>5nk4A (length=290) Species: 9606 (Homo sapiens) [Search protein sequence]
VLKFTTEIHPSCVTRQKVIGAGEFGEVYKGMLKEVPVAIKTLKAGYTEKQ
RVDFLGEAGIMGQFSHHNIIRLEGVISKYKPMMIITEYMENGALDKFLRE
KDGEFSVLQLVGMLRGIAAGMKYLANMNYVHRDLAARNILVNSNLVCKVS
DFGLSRVLEDDPEATYTTSGGKIPIRWTAPEAISYRKFTSASDVWSFGIV
MWEVMTYGERPYWELSNHEVMKAINDGFRLPTPMDCPSAIYQLMMQCWQQ
ERARRPKFADIVSILDKLIRAPDSLKTLADFDPRVSIRLP
3D structure
PDB5nk4 Chemoproteomics-Aided Medicinal Chemistry for the Discovery of EPHA2 Inhibitors.
ChainA
Resolution1.45 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) D133 A135 R137 N138 D151 D160 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 90E A I619 A644 I645 K646 E663 I690 T692 Y694 M695 E696 N697 G698 L746 I19 A38 I39 K40 E57 I84 T86 Y88 M89 E90 N91 G92 L140 MOAD: Kd=1.995nM
PDBbind-CN: -logKd/Ki=8.70,Kd=2.0nM
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:5nk4, PDBe:5nk4, PDBj:5nk4
PDBsum5nk4
PubMed28544567
UniProtP29317|EPHA2_HUMAN Ephrin type-A receptor 2 (Gene Name=EPHA2)

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