X-ray diffraction
1.64Å resolution

Crystal structure of KRas G12V/D38P, bound to GDP


Function and Biology Details

Reaction catalysed:
GTP + H(2)O = GDP + phosphate
Biochemical function:
  • not assigned
Biological process:
  • not assigned
Cellular component:
  • not assigned

Structure analysis Details

Assemblies composition:
monomeric (preferred)
homo dimer
Entry contents:
1 distinct polypeptide molecule
GTPase KRas, N-terminally processed; Isoform 2B of GTPase KRas Chains: A, B, C, D
Molecule details ›
Chains: A, B, C, D
Length: 170 amino acids
Theoretical weight: 19.14 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
  • Canonical: P01116 (Residues: 1-166; Coverage: 88%)
  • Best match: P01116-2 (Residues: 1-166)
Gene names: KRAS, KRAS2, RASK2
Sequence domains: Ras family
Structure domains: P-loop containing nucleotide triphosphate hydrolases

Ligands and Environments

1 bound ligand:
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 24-ID-E
Spacegroup: P21
Unit cell:
a: 37.239Å b: 80.912Å c: 108.041Å
α: 90° β: 90.62° γ: 90°
R R work R free
0.194 0.192 0.225
Expression system: Escherichia coli