Structure of PDB 2vwy Chain A

Receptor sequence
>2vwyA (length=274) Species: 9606 (Homo sapiens) [Search protein sequence]
KEIDVSYVKIEEVIGAGEFGEVCRGRLKAPGKKESCVAIKTLKGGYTERQ
RREFLSEASIMGQFEHPNIIRLEGVVTNSMPVMILTEFMENGALDSFLRL
NDGQFTVIQLVGMLRGIASGMRYLAEMSYVHRDLAARNILVNSNLVCKVS
DFGLSRFLEENSSDGGKIPIRWTAPEAIAFRKFTSASDAWSYGIVMWEVM
SFGERPYWDMSNQDVINAIEQDYRLPPPPDCPTSLHQLMLDCWQKDRNAR
PRFPQVVSALDKMIRNPASLKIVA
3D structure
PDB2vwy Inhibitors of the Tyrosine Kinase Ephb4. Part 2: Structure-Based Discovery and Optimisation of 3,5-Bis Substituted Anilinopyrimidines.
ChainA
Resolution1.65 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) D740 A742 R744 N745 D758 K781 P783
Catalytic site (residue number reindexed from 1) D133 A135 R137 N138 D151 K167 P169
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 7X5 A I621 A645 K647 E664 I691 T693 M696 G699 L747 S757 I14 A38 K40 E57 I84 T86 M89 G92 L140 S150 MOAD: ic50=0.09uM
PDBbind-CN: -logKd/Ki=7.05,IC50=0.09uM
BindingDB: IC50=90nM
BS02 MG A D740 D758 D133 D151
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:2vwy, PDBe:2vwy, PDBj:2vwy
PDBsum2vwy
PubMed18851911
UniProtP54760|EPHB4_HUMAN Ephrin type-B receptor 4 (Gene Name=EPHB4)

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