Structure of PDB 4p5z Chain A

Receptor sequence
>4p5zA (length=267) Species: 9606 (Homo sapiens) [Search protein sequence]
VHEFAKELDATNISIDKVVGAGEFGEVCSGRLKLPSKKEISVAIKTLKVG
YTEKQRRDFLGEASIMGQFDHPNIIRLEGVVTKSKPVMIVTEYMENGSLD
SFLRKHDAQFTVIQLVGMLRGIASGMKYLSDMGYVHRDLAARNILINSNL
VCKVSDFPIRWTSPEAIAYRKFTSASDVWSYGIVLWEVMSYGERPYWEMS
NQDVIKAVDEGYRLPPPMDCPAALYQLMLDCWQKDRNNRPKFEQIVSILD
KLIRNPGSLKIITNLLL
3D structure
PDB4p5z Pyrrolo[3,2-b]quinoxaline Derivatives as Types I1/2 and II Eph Tyrosine Kinase Inhibitors: Structure-Based Design, Synthesis, and in Vivo Validation.
ChainA
Resolution2.002 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) D746 A748 R750 N751 D764
Catalytic site (residue number reindexed from 1) D138 A140 R142 N143 D156
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 Q7M A V635 A651 K653 E670 I673 M674 F677 I683 M702 Y742 L753 S763 D764 F765 V27 A43 K45 E62 I65 M66 F69 I75 M94 Y134 L145 S155 D156 F157 MOAD: Kd=39.3nM
PDBbind-CN: -logKd/Ki=7.41,Kd=39.3nM
BindingDB: Kd=3.9nM
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:4p5z, PDBe:4p5z, PDBj:4p5z
PDBsum4p5z
PubMed25076195
UniProtP29320|EPHA3_HUMAN Ephrin type-A receptor 3 (Gene Name=EPHA3)

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