We've built a new version of this page with an interactive 3D viewer. Try it out in beta and help us improve:

› 7o70

X-ray diffraction
1.18Å resolution

Function and Biology Details

Reaction catalysed: 
GTP + H2O = GDP + phosphate + H(+).
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, D
Molecule details ›
Chains: A, D
Length: 170 amino acids
Theoretical weight: 19.35 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: P01116 (Residues: 1-169; Coverage: 89%)
  • Best match: P01116-2 (Residues: 1-169)
Gene names: KRAS, KRAS2, RASK2
Sequence domains: Ras family

Ligands and Environments

4 bound ligands:
Ligand V4T 2 x V4T
Ligand MG 2 x MG
Ligand GDP 2 x GDP
Ligand CA 2 x CA
No modified residues

Experiments and Validation Details

wwPDB Validation report is not available for this entry.
X-ray source: DIAMOND BEAMLINE I04
Spacegroup: P21
Unit cell:
a: 33.38Å b: 70.46Å c: 66.15Å
α: 90° β: 90.26° γ: 90°
R-values:
R R work R free
0.227 0.226 0.257
Expression system: Escherichia coli

Quick links

Citations

2 review citations

Multiple Strategies to Develop Small Molecular KRAS Directly Bound Inhibitors.
Zhou et al. (2023)
1 more

1 mention without citation

In Silico Evaluation of the Thr58-Associated Conserved Water with KRAS Switch-II Pocket Binders.
Leini et al. (2023)