› 5v9o

X-ray diffraction
1.56Å resolution

KRAS G12C inhibitor

Released:
DOI: 10.2210/pdb5v9o/pdb
PDB entry 5v9o coloured by chain, front view.
PDB entry 5v9o coloured by chain, side view.
PDB entry 5v9o coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Potent and Selective Covalent Quinazoline Inhibitors of KRAS G12C.
Zeng M, Lu J, Li L, Feru F, Quan C, Gero TW, Ficarro SB, Xiong Y, Ambrogio C, Paranal RM, Catalano M, Shao J, Wong KK, Marto JA, Fischer ES, Jänne PA, Scott DA, Westover KD, Gray NS
Cell Chem Biol 24 1005-1016.e3 (2017)
PMID: 28781124

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 Chain: A
Molecule details ›
Chain: A
Length: 169 amino acids
Theoretical weight: 19.25 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli K-12
UniProt:
  • Canonical: P01116 (Residues: 1-167; Coverage: 88%)
Gene names: KRAS, KRAS2, RASK2
Sequence domains: Ras family
Structure domains: P-loop containing nucleotide triphosphate hydrolases

Ligands and Environments

3 bound ligands:
Ligand GDP 1 x GDP
Ligand MG 1 x MG
Ligand 91G 1 x 91G
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 19-ID
Spacegroup: P23
Unit cell:
a: 90.159Å b: 90.159Å c: 90.159Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.182 0.18 0.199
Expression system: Escherichia coli K-12

Quick links

Citations

22 review citations

Therapeutic strategies to target RAS-mutant cancers.
Ryan et al. (2018)
21 more

8 mentions without citation

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