› 6e6h

X-ray diffraction
1.99Å resolution

Function and Biology Details

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

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-524678 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
GTPase NRas 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: P01111 (Residues: 1-166; Coverage: 88%)
Gene names: HRAS1, NRAS
Sequence domains: Ras family

Ligands and Environments

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

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU MICROMAX-007 HF
Spacegroup: C2
Unit cell:
a: 59.553Å b: 39.565Å c: 65.016Å
α: 90° β: 106.4° γ: 90°
R-values:
R R work R free
0.179 0.179 0.236
Expression system: Escherichia coli BL21

Quick links

Citations

10 review citations

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

1 mention without citation

Isoform-Specific Destabilization of the Active Site Reveals a Molecular Mechanism of Intrinsic Activation of KRas G13D.
Johnson et al. (2019)