› 6pgo

X-ray diffraction
1.6Å 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: 183 amino acids
Theoretical weight: 21.04 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: P01116 (Residues: 1-169; Coverage: 89%)
Gene names: KRAS, KRAS2, RASK2
Sequence domains: Ras family

Ligands and Environments

3 bound ligands:
Ligand MG 2 x MG
Ligand GDP 2 x GDP
Ligand OJ1 2 x OJ1
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 22-ID
Spacegroup: P21212
Unit cell:
a: 79.565Å b: 106.329Å c: 33.736Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.218 0.217 0.231
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

67 review citations

Expanding the Reach of Precision Oncology by Drugging All KRAS Mutants.
Hofmann et al. (2022)
66 more

2 mentions without citation

Cryo-EM structure determination of small therapeutic protein targets at 3 Å-resolution using a rigid imaging scaffold.
Castells-Graells et al. (2023)
1 more