Structure of PDB 2hen Chain D

Receptor sequence
>2henD (length=259) Species: 10090 (Mus musculus) [Search protein sequence]
SKEIDISCVKIEQVIGAGEFGEVCSGHLKLPGKREIFVAIKTLKSGYTEK
QRRDFLSEASIMGQFDHPNVIHLEGVVTKSTPVMIITEFMENGSLDSFLR
QNDGQFTVIQLVGMLRGIAAGMKYLADMNYVHRALAARNILVNSNLVCKV
SDFGPIRWTAPEAIQYRKFTSASDVWSYGIVMWEVMSYGERPYWDMTNQD
VINAIEQDYRLPPPMDCPSALHQLMLDCWQKDRNHRPKFGQIVNTLDKMI
RNPNSLKAM
3D structure
PDB2hen A change in conformational dynamics underlies the activation of Eph receptor tyrosine kinases
ChainD
Resolution2.6 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) A754 A756 R758 N759 D772
Catalytic site (residue number reindexed from 1) A134 A136 R138 N139 D152
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 ADP D I635 E639 V643 A659 K661 F709 M710 S714 L761 I15 E19 V23 A39 K41 F89 M90 S94 L141
Gene Ontology
Molecular Function
GO:0004672 protein kinase activity
GO:0005524 ATP binding
Biological Process
GO:0006468 protein phosphorylation

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Molecular Function
View graph for
Biological Process
External links
PDB RCSB:2hen, PDBe:2hen, PDBj:2hen
PDBsum2hen
PubMed16977320
UniProtP54763|EPHB2_MOUSE Ephrin type-B receptor 2 (Gene Name=Ephb2)

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