5vp7

X-ray diffraction
1.7Å resolution

Crystal structure of human KRAS G12A mutant in complex with GDP

Released:
Source organism: Homo sapiens
Primary publication:
Structural insight into the rearrangement of the switch I region in GTP-bound G12A K-Ras.
Acta Crystallogr D Struct Biol 73 970-984 (2017)
PMID: 29199977

Function and Biology Details

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

Structure analysis Details

Assembly composition:
monomeric (preferred)
PDBe Complex ID:
PDB-CPX-133991 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
GTPase KRas, N-terminally processed Chains: A, F
Molecule details ›
Chains: A, F
Length: 170 amino acids
Theoretical weight: 19.41 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: P01116 (Residues: 1-169; Coverage: 89%)
Gene names: KRAS, KRAS2, RASK2
Sequence domains: Ras family
Structure domains: P-loop containing nucleotide triphosphate hydrolases

Ligands and Environments

No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 31-ID
Spacegroup: R3
Unit cell:
a: 93.773Å b: 93.773Å c: 119.918Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.173 0.171 0.207
Expression system: Escherichia coli