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X-ray diffraction
1.48Å 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, D
Molecule details ›
Chains: A, D
Length: 169 amino acids
Theoretical weight: 19.22 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: P01116 (Residues: 1-164; Coverage: 87%)
Gene names: KRAS, KRAS2, RASK2
Sequence domains: Ras family

Ligands and Environments

4 bound ligands:
Ligand MG 2 x MG
Ligand GDP 2 x GDP
Ligand VLE 2 x VLE
Ligand CA 1 x CA
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: DIAMOND BEAMLINE I03
Spacegroup: P21
Unit cell:
a: 33.289Å b: 72.012Å c: 65.821Å
α: 90° β: 90.32° γ: 90°
R-values:
R R work R free
0.192 0.19 0.226
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)