› 2rgd

X-ray diffraction
2Å resolution

Crystal structure of H-RasQ61L-GppNHp

Released:
DOI: 10.2210/pdb2rgd/pdb
PDB entry 2rgd coloured by chain, front view.
PDB entry 2rgd coloured by chain, side view.
PDB entry 2rgd coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Transformation efficiency of RasQ61 mutants linked to structural features of the switch regions in the presence of Raf.
Buhrman G, Wink G, Mattos C
Structure 15 1618-29 (2007)
PMID: 18073111

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

3 bound ligands:
Ligand CA 1 x CA
Ligand MG 2 x MG
Ligand GNP 1 x GNP
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 22-ID
Spacegroup: R32
Unit cell:
a: 88.953Å b: 88.953Å c: 134.022Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.184 0.184 0.22
Expression system: Escherichia coli BL21

Quick links

Citations

12 review citations

RAS isoforms and mutations in cancer at a glance.
Hobbs et al. (2016)
11 more

7 mentions without citation

Allosteric effects of the oncogenic RasQ61L mutant on Raf-RBD.
Fetics et al. (2015)
6 more