› 2x11

X-ray diffraction
4.83Å resolution

Crystal structure of the complete EphA2 ectodomain in complex with ephrin A5 receptor binding domain

Released:
DOI: 10.2210/pdb2x11/pdb
PDB entry 2x11 coloured by chain, front view.
PDB entry 2x11 coloured by chain, side view.
PDB entry 2x11 coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
An extracellular steric seeding mechanism for Eph-ephrin signaling platform assembly.
Seiradake E, Harlos K, Sutton G, Aricescu AR, Jones EY
Nat Struct Mol Biol 17 398-402 (2010)
PMID: 20228801

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 analysis Details

Assembly composition:
hetero dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-151388 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Ephrin type-A receptor 2 Chain: A
Molecule details ›
Chain: A
Length: 545 amino acids
Theoretical weight: 59.86 KDa
Source organism: Homo sapiens
Expression system: Homo sapiens
UniProt:
  • Canonical: P29317 (Residues: 11-534; Coverage: 53%)
Gene names: ECK, EPHA2
Sequence domains:
Ephrin-A5 Chain: B
Molecule details ›
Chain: B
Length: 177 amino acids
Theoretical weight: 20.4 KDa
Source organism: Homo sapiens
Expression system: Homo sapiens
UniProt:
  • Canonical: P52803 (Residues: 4-171; Coverage: 69%)
Gene names: EFNA5, EPLG7, LERK7
Sequence domains: Ephrin

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE ID14-2
Spacegroup: P2221
Unit cell:
a: 173.63Å b: 59.63Å c: 112.16Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.313 0.312 0.314
Expression system: Homo sapiens

Quick links

Citations

43 review citations

Cell signaling by receptor tyrosine kinases.
Lemmon et al. (2010)
42 more

6 mentions without citation

Cells under siege: viral glycoprotein interactions at the cell surface.
Bowden et al. (2011)
5 more