› 1u8y

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

Released:
DOI: 10.2210/pdb1u8y/pdb
PDB entry 1u8y coloured by chain, front view.
PDB entry 1u8y coloured by chain, side view.
PDB entry 1u8y coloured by chain, top view.
Source organism: Saguinus oedipus
Primary publication:
Crystal structures of Ral-GppNHp and Ral-GDP reveal two binding sites that are also present in Ras and Rap.
Nicely NI, Kosak J, de Serrano V, Mattos C
Structure 12 2025-36 (2004)
PMID: 15530367

Function and Biology Details

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

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-159092 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
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
UniProt:
  • 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:
Ligand MG 4 x MG
Ligand GNP 2 x GNP
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-values:
R R work R free
0.213 0.213 0.238
Expression system: Escherichia coli

Quick links

Citations

6 review citations

Structure-function relationships of the G domain, a canonical switch motif.
Wittinghofer et al. (2011)
5 more

5 mentions without citation

Revealing conformational substates of lipidated N-Ras protein by pressure modulation.
Kapoor et al. (2012)
4 more