› 2qbx

X-ray diffraction
2.3Å resolution

EphB2/SNEW Antagonistic Peptide Complex

Released:
DOI: 10.2210/pdb2qbx/pdb
PDB entry 2qbx coloured by chain, front view.
PDB entry 2qbx coloured by chain, side view.
PDB entry 2qbx coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Three-dimensional structure of the EphB2 receptor in complex with an antagonistic peptide reveals a novel mode of inhibition.
Chrencik JE, Brooun A, Recht MI, Nicola G, Davis LK, Abagyan R, Widmer H, Pasquale EB, Kuhn P
J Biol Chem 282 36505-13 (2007)
PMID: 17897949

Function and Biology Details

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

Structure analysis Details

Assemblies composition:
hetero dimer (preferred)
hetero tetramer
Assembly name:
PDBe Complex ID:
PDB-CPX-151406 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Ephrin type-B receptor 2 Chains: A, B
Molecule details ›
Chains: A, B
Length: 208 amino acids
Theoretical weight: 23.66 KDa
Source organism: Homo sapiens
Expression system: Spodoptera frugiperda
UniProt:
  • Canonical: P29323 (Residues: 20-196; Coverage: 17%)
Gene names: DRT, EPHB2, EPHT3, EPTH3, ERK, HEK5, TYRO5
Sequence domains: Ephrin receptor ligand binding domain
Structure domains: Galactose-binding domain-like
antagonistic peptide Chains: D, P
Molecule details ›
Chains: D, P
Length: 12 amino acids
Theoretical weight: 1.51 KDa
Source organism: Homo sapiens
Expression system: Not provided

Ligands and Environments

1 bound ligand:
Ligand SO4 12 x SO4
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 23-ID-D
Spacegroup: P32
Unit cell:
a: 40.183Å b: 40.183Å c: 235.025Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.198 0.194 0.27
Expression systems:
  • Spodoptera frugiperda
  • Not provided

Quick links

Citations

11 review citations

Eph receptors and ephrins in cancer: bidirectional signalling and beyond.
Pasquale EB. (2010)
10 more

6 mentions without citation

Targeting the Eph System with Peptides and Peptide Conjugates.
Riedl et al. (2015)
5 more