› 1nuk

X-ray diffraction
2.9Å resolution

CRYSTAL STRUCTURE OF THE LIGAND-BINDING DOMAIN OF THE EPHB2 RECEPTOR TYROSINE KINASE

Released:
DOI: 10.2210/pdb1nuk/pdb
PDB entry 1nuk coloured by chain, front view.
PDB entry 1nuk coloured by chain, side view.
PDB entry 1nuk coloured by chain, top view.
Source organism: Mus musculus
Primary publication:
Crystal structure of the ligand-binding domain of the receptor tyrosine kinase EphB2.
Himanen JP, Henkemeyer M, Nikolov DB
Nature 396 486-91 (1998)
PMID: 9853759

Function and Biology Details

Reaction catalysed: 
ATP + a [protein]-L-tyrosine = ADP + a [protein]-L-tyrosine phosphate
Biochemical function:
Biological process:
Cellular component:
Sequence domains:
Structure domain:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-157093 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Ephrin type-B receptor 2 Chain: A
Molecule details ›
Chain: A
Length: 183 amino acids
Theoretical weight: 21.14 KDa
Source organism: Mus musculus
Expression system: Escherichia coli
UniProt:
  • Canonical: P54763 (Residues: 20-202; Coverage: 19%)
Gene names: Ephb2, Epth3, Nuk, Sek3
Sequence domains: Ephrin receptor ligand binding domain
Structure domains: Galactose-binding domain-like

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU RU200
Spacegroup: P41212
Unit cell:
a: 55.15Å b: 55.15Å c: 158.9Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.206 0.206 0.314
Expression system: Escherichia coli

Quick links

Citations

21 review citations

Mechanisms and functions of Eph and ephrin signalling.
Kullander et al. (2002)
20 more

6 mentions without citation

Crystal structure and carbohydrate analysis of Nipah virus attachment glycoprotein: a template for antiviral and vaccine design.
Bowden et al. (2008)
5 more