› 5uhv

X-ray diffraction
1.67Å resolution

wild-type NRas bound to GppNHp

Released:
DOI: 10.2210/pdb5uhv/pdb
PDB entry 5uhv coloured by chain, front view.
PDB entry 5uhv coloured by chain, side view.
PDB entry 5uhv coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
The small GTPases K-Ras, N-Ras, and H-Ras have distinct biochemical properties determined by allosteric effects.
Johnson CW, Reid D, Parker JA, Salter S, Knihtila R, Kuzmic P, Mattos C
J Biol Chem 292 12981-12993 (2017)
PMID: 28630043

Function and Biology Details

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

Structure analysis Details

Assemblies composition:
monomeric (preferred)
homo dimer
Assembly name:
PDBe Complex ID:
PDB-CPX-133953 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
GTPase NRas Chain: A
Molecule details ›
Chain: A
Length: 166 amino acids
Theoretical weight: 18.8 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: P01111 (Residues: 1-166; Coverage: 88%)
Gene names: HRAS1, NRAS
Sequence domains: Ras family
Structure domains: P-loop containing nucleotide triphosphate hydrolases

Ligands and Environments

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

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU MICROMAX-007 HF
Spacegroup: P3221
Unit cell:
a: 39.007Å b: 39.007Å c: 159.175Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.191 0.187 0.226
Expression system: Escherichia coli

Quick links

Citations

12 review citations

The Frequency of Ras Mutations in Cancer.
Prior et al. (2020)
11 more

19 mentions without citation

The K-Ras, N-Ras, and H-Ras Isoforms: Unique Conformational Preferences and Implications for Targeting Oncogenic Mutants.
Parker et al. (2018)
18 more