› 1lf5

X-ray diffraction
1.7Å resolution

Crystal Structure of RasA59G in the GDP-bound Form

Released:
DOI: 10.2210/pdb1lf5/pdb
PDB entry 1lf5 coloured by chain, front view.
PDB entry 1lf5 coloured by chain, side view.
PDB entry 1lf5 coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
The structural basis for the transition from Ras-GTP to Ras-GDP.
Hall BE, Bar-Sagi D, Nassar N
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:
Sequence domains:
Structure domain:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-133956 (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

2 bound ligands:
Ligand MG 1 x MG
Ligand GDP 1 x GDP
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: NSLS BEAMLINE X26C
Spacegroup: R32
Unit cell:
a: 93.112Å b: 93.112Å c: 120.301Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.222 0.222 0.245
Expression system: Escherichia coli BL21

Quick links

Citations

21 review citations

CHARMM: the biomolecular simulation program.
Brooks et al. (2009)
20 more

4 mentions without citation

The distinct conformational dynamics of K-Ras and H-Ras A59G.
Lukman et al. (2010)
3 more