5w22

X-ray diffraction
1.76Å resolution

Crystal structure of human WT-KRAS 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, B
Molecule details ›
Chains: A, B
Length: 170 amino acids
Theoretical weight: 19.39 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

2 bound ligands:
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 31-ID
Spacegroup: R3
Unit cell:
a: 93.177Å b: 93.177Å c: 118.431Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.179 0.177 0.204
Expression system: Escherichia coli