X-ray diffraction
2.51Å resolution

Crystal Structure of unliganded Argos

Source organism: Drosophila melanogaster
Primary publication:
Structural basis for EGFR ligand sequestration by Argos.
Nature 453 1271-5 (2008)
PMID: 18500331

Function and Biology Details

Biochemical function:
  • not assigned
Biological process:
  • not assigned
Cellular component:
  • not assigned

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Entry contents:
1 distinct polypeptide molecule
Protein giant-lens Chains: A, B
Molecule details ›
Chains: A, B
Length: 223 amino acids
Theoretical weight: 25.62 KDa
Source organism: Drosophila melanogaster
Expression system: Spodoptera frugiperda
  • Canonical: Q00805 (Residues: 113-165, 285-444; Coverage: 51%)
Gene names: CG4531, aos, gil, sty
Sequence domains: Antagonist of EGFR signalling, Argos
Structure domains:

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ALS BEAMLINE 8.2.1
Spacegroup: C2
Unit cell:
a: 113.583Å b: 64.246Å c: 72.53Å
α: 90° β: 101.59° γ: 90°
R R work R free
0.258 0.256 0.299
Expression system: Spodoptera frugiperda