› 6e6f

X-ray diffraction
3.4Å 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-133991 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
GTPase KRas, N-terminally processed Chains: A, B
Molecule details ›
Chains: A, B
Length: 166 amino acids
Theoretical weight: 18.94 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21
UniProt:
  • Canonical: P01116 (Residues: 1-166; Coverage: 88%)
Gene names: KRAS, KRAS2, RASK2
Sequence domains: Ras family

Ligands and Environments

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

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU MICROMAX-007 HF
Spacegroup: C2
Unit cell:
a: 114.486Å b: 39.096Å c: 89.319Å
α: 90° β: 124.37° γ: 90°
R-values:
R R work R free
0.187 0.182 0.258
Expression system: Escherichia coli BL21

Quick links

Citations

10 review citations

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

2 mentions without citation

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