› 4w50

X-ray diffraction
2.42Å resolution

Structure of the EphA4 LBD in complex with peptide

Released:
DOI: 10.2210/pdb4w50/pdb
PDB entry 4w50 coloured by chain, front view.
PDB entry 4w50 coloured by chain, side view.
PDB entry 4w50 coloured by chain, top view.
Source organisms:
Primary publication:
Development and structural analysis of a nanomolar cyclic peptide antagonist for the EphA4 receptor.
Lamberto I, Lechtenberg BC, Olson EJ, Mace PD, Dawson PE, Riedl SJ, Pasquale EB
ACS Chem Biol 9 2787-95 (2014)
PMID: 25268696

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

Assembly composition:
hetero dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-157096 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Ephrin type-A receptor 4 Chains: A, B, C, D
Molecule details ›
Chains: A, B, C, D
Length: 179 amino acids
Theoretical weight: 20.49 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: P54764 (Residues: 29-204; Coverage: 18%)
Gene names: EPHA4, HEK8, SEK, TYRO1
Sequence domains: Ephrin receptor ligand binding domain
Structure domains: Galactose-binding domain-like
APY peptide Chains: E, F, G, H
Molecule details ›
Chains: E, F, G, H
Length: 12 amino acids
Theoretical weight: 1.39 KDa
Source organism: synthetic construct
Expression system: Not provided

Ligands and Environments

2 bound ligands:
Ligand BU2 4 x BU2
Ligand GOL 6 x GOL
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU FR-E SUPERBRIGHT
Spacegroup: P21
Unit cell:
a: 36.27Å b: 127.69Å c: 84.569Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.174 0.171 0.232
Expression systems:
  • Escherichia coli
  • Not provided

Quick links

Citations

8 review citations

High-Throughput Screening by Nuclear Magnetic Resonance (HTS by NMR) for the Identification of PPIs Antagonists.
Wu et al. (2015)
7 more

2 mentions without citation

Structural insights into EphA4 unconventional activation from prediction of the EphA4 and its complex with ribonuclease 1.
Li et al. (2022)
1 more