› 2hel

X-ray diffraction
2.35Å resolution

Crystal structure of a mutant EphA4 kinase domain (Y742A)

Released:
DOI: 10.2210/pdb2hel/pdb
PDB entry 2hel coloured by chain, front view.
PDB entry 2hel coloured by chain, side view.
PDB entry 2hel 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-169846 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Ephrin type-A receptor 4 Chain: A
Molecule details ›
Chain: A
Length: 306 amino acids
Theoretical weight: 34.58 KDa
Source organism: Mus musculus
Expression system: Escherichia coli
UniProt:
  • Canonical: Q03137 (Residues: 591-896; Coverage: 32%)
Gene names: Epha4, Sek, Sek1
Sequence domains:
Structure domains:

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU
Spacegroup: P21
Unit cell:
a: 32.283Å b: 101.081Å c: 40.95Å
α: 90° β: 108.8° γ: 90°
R-values:
R R work R free
0.209 0.209 0.248
Expression system: Escherichia coli

Quick links

Citations

20 review citations

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