1lf0

X-ray diffraction
1.7Å resolution

Crystal Structure of RasA59G in the GTP-bound form

Released:
Source organism: Homo sapiens
Primary publication:
The structural basis for the transition from Ras-GTP to Ras-GDP.
Proc. Natl. Acad. Sci. U.S.A. 99 12138-42 (2002)
PMID: 12213964

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
Macromolecule:
GTPase HRas, N-terminally processed Chain: A
Molecule details ›
Chain: A
Length: 166 amino acids
Theoretical weight: 18.86 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21
UniProt:
  • Canonical: P01112 (Residues: 1-166; Coverage: 88%)
Gene names: HRAS, HRAS1
Sequence domains: Ras family
Structure domains: P-loop containing nucleotide triphosphate hydrolases

Ligands and Environments

3 bound ligands:
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: NSLS BEAMLINE X26C
Spacegroup: R32
Unit cell:
a: 89.129Å b: 89.129Å c: 134.654Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.185 0.185 0.208
Expression system: Escherichia coli BL21