› 5o2t

X-ray diffraction
2.19Å 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:
hetero dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-134004 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
GTPase KRas, N-terminally processed Chain: A
Molecule details ›
Chain: A
Length: 169 amino acids
Theoretical weight: 19.21 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: P01116 (Residues: 1-166; Coverage: 88%)
Gene names: KRAS, KRAS2, RASK2
Sequence domains: Ras family
Structure domains: P-loop containing nucleotide triphosphate hydrolases
darpin 55 Chain: B
Molecule details ›
Chain: B
Length: 187 amino acids
Theoretical weight: 20.44 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
Structure domains: Ankyrin repeat-containing domain

Ligands and Environments

3 bound ligands:
Ligand MG 1 x MG
Ligand GSP 1 x GSP
Ligand SO4 2 x SO4
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: DIAMOND BEAMLINE I04
Spacegroup: R3
Unit cell:
a: 112.83Å b: 112.83Å c: 66.77Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.184 0.182 0.229
Expression system: Escherichia coli

Quick links

Citations

17 review citations

RAS, wanted dead or alive: Advances in targeting RAS mutant cancers.
Stalnecker et al. (2020)
16 more

4 mentions without citation

Structure-based inhibitor design of mutant RAS proteins-a paradigm shift.
Nyíri et al. (2020)
3 more