X-ray diffraction
1.8Å resolution

Crystal Structure of human Rad GTPase

Source organism: Homo sapiens
Primary publication:
Crystal structure of human Rad GTPase of the RGK-family.
Genes Cells 11 961-8 (2006)
PMID: 16866878

Function and Biology Details

Reaction catalysed:
GTP + H(2)O = GDP + phosphate
Biochemical function:
Cellular component:
  • not assigned

Structure analysis Details

Assembly composition:
monomeric (preferred)
Entry contents:
1 distinct polypeptide molecule
GTP-binding protein RAD Chains: A, B
Molecule details ›
Chains: A, B
Length: 174 amino acids
Theoretical weight: 19.05 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
  • Canonical: P55042 (Residues: 87-258; Coverage: 56%)
Gene names: RAD, RRAD
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: SPRING-8 BEAMLINE BL41XU
Spacegroup: P21
Unit cell:
a: 52.163Å b: 58.608Å c: 53.44Å
α: 90° β: 97.98° γ: 90°
R R work R free
0.214 0.214 0.24
Expression system: Escherichia coli