› 5v6v

X-ray diffraction
1.72Å resolution

Crystal structure of small molecule aziridine 3 covalently bound to K-Ras G12C

Released:
DOI: 10.2210/pdb5v6v/pdb
PDB entry 5v6v coloured by chain, front view.
PDB entry 5v6v coloured by chain, side view.
PDB entry 5v6v coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Expanding the Scope of Electrophiles Capable of Targeting K-Ras Oncogenes.
McGregor LM, Jenkins ML, Kerwin C, Burke JE, Shokat KM
Biochemistry 56 3178-3183 (2017)
PMID: 28621541

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:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-134027 (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: 19.35 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

4 bound ligands:
Ligand GDP 2 x GDP
Ligand CA 6 x CA
Ligand 8YA 2 x 8YA
Ligand GOL 1 x GOL
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ALS BEAMLINE 8.2.2
Spacegroup: P1
Unit cell:
a: 33.23Å b: 39.17Å c: 62.34Å
α: 77.34° β: 81.44° γ: 76.86°
R-values:
R R work R free
0.17 0.168 0.202
Expression system: Escherichia coli

Quick links

Citations

8 review citations

The current understanding of KRAS protein structure and dynamics.
Pantsar T. (2020)
7 more

5 mentions without citation

Expanding the Scope of Electrophiles Capable of Targeting K-Ras Oncogenes.
McGregor et al. (2017)
4 more