› 2hen

X-ray diffraction
2.6Å resolution

Crystal Structure of the EphB2 Receptor Kinase domain in complex with ADP

Released:
DOI: 10.2210/pdb2hen/pdb
PDB entry 2hen coloured by chain, front view.
PDB entry 2hen coloured by chain, side view.
PDB entry 2hen coloured by chain, top view.
Source organism: Mus musculus
Primary publication:
A change in conformational dynamics underlies the activation of Eph receptor tyrosine kinases.
Wiesner S, Wybenga-Groot LE, Warner N, Lin H, Pawson T, Forman-Kay JD, Sicheri F
EMBO J 25 4686-96 (2006)
PMID: 16977320

Function and Biology Details

Reaction catalysed: 
ATP + a [protein]-L-tyrosine = ADP + a [protein]-L-tyrosine phosphate
Biochemical function:
Biological process:
Cellular component:
  • not assigned
Sequence domains:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-157093 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
EphB2/CTF2 Chains: A, B, C, D
Molecule details ›
Chains: A, B, C, D
Length: 286 amino acids
Theoretical weight: 32.29 KDa
Source organism: Mus musculus
Expression system: Escherichia coli
UniProt:
  • Canonical: P54763 (Residues: 614-898; Coverage: 29%)
Gene names: Ephb2, Epth3, Nuk, Sek3
Sequence domains: Protein tyrosine and serine/threonine kinase
Structure domains:

Ligands and Environments

2 bound ligands:
Ligand MG 4 x MG
Ligand ADP 4 x ADP
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU
Spacegroup: P21
Unit cell:
a: 60.798Å b: 98.304Å c: 114.168Å
α: 90° β: 90.18° γ: 90°
R-values:
R R work R free
0.205 0.205 0.26
Expression system: Escherichia coli

Quick links

Citations

20 review citations

Bidirectional Eph-ephrin signaling during axon guidance.
Egea et al. (2007)
19 more

5 mentions without citation

Using multiple microenvironments to find similar ligand-binding sites: application to kinase inhibitor binding.
Liu et al. (2011)
4 more