X-ray diffraction
1.55Å resolution

CRystal structures of Ral-GppNHp and Ral-GDP reveal two novel binding sites that are also present in Ras and Rap


Function and Biology Details

Reaction catalysed:
GTP + H(2)O = GDP + phosphate
Biochemical function:
Biological process:
Cellular component:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Entry contents:
1 distinct polypeptide molecule
Ras-related protein Ral-A Chains: A, B
Molecule details ›
Chains: A, B
Length: 168 amino acids
Theoretical weight: 19.18 KDa
Source organism: Saguinus oedipus
Expression system: Escherichia coli
  • Canonical: P63320 (Residues: 11-178; Coverage: 82%)
Gene names: RAL, RALA
Sequence domains: Ras family
Structure domains: P-loop containing nucleotide triphosphate hydrolases

Ligands and Environments

2 bound ligands:
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 19-ID
Spacegroup: P4222
Unit cell:
a: 77.318Å b: 77.318Å c: 116.134Å
α: 90° β: 90° γ: 90°
R R work R free
0.213 0.213 0.238
Expression system: Escherichia coli