Structure of PDB 2xyu Chain A

Receptor sequence
>2xyuA (length=260) Species: 10090 (Mus musculus) [Search protein sequence]
FAKEIDASCIKIEKVIGVGEFGEVCSGRLKVPGKREICVAIKTLKAGYTD
KQRRDFLSEASIMGQFDHPNIIHLEGVVTKCKPVMIITEYMENGSLDAFL
RKNDGRFTVIQLVGMLRGIGSGMKYLSDMSYVHRDLAARNILVNSNLVCK
VSDFIPIRWTAPEAIAYRKFTSASDVWSYGIVMWEVMSYGERPYWDMSNQ
DVIKAIEEGYRLPPPMDCPIALHQLMLDCWQKERSDRPKFGQIVNMLDKL
IRNPNSLKRT
3D structure
PDB2xyu Fragment Based Lead Discovery of Small Molecule Inhibitors for the Epha4 Receptor Tyrosine Kinase.
ChainA
Resolution2.117 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) D746 A748 R750 N751 D764 I786
Catalytic site (residue number reindexed from 1) D135 A137 R139 N140 D153 I155
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 Q9G A A651 K653 M674 T699 Y701 M702 L753 S763 A40 K42 M63 T88 Y90 M91 L142 S152 MOAD: ic50=4.5uM
PDBbind-CN: -logKd/Ki=5.35,IC50=4.5uM
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:2xyu, PDBe:2xyu, PDBj:2xyu
PDBsum2xyu
PubMed22137457
UniProtQ03137|EPHA4_MOUSE Ephrin type-A receptor 4 (Gene Name=Epha4)

[Back to BioLiP]