› 5ufe

X-ray diffraction
2.3Å resolution

Wild-type K-Ras(GNP)/R11.1.6 complex

Released:
DOI: 10.2210/pdb5ufe/pdb
PDB entry 5ufe coloured by chain, front view.
PDB entry 5ufe coloured by chain, side view.
PDB entry 5ufe coloured by chain, top view.
Source organisms:
Primary publication:
An engineered protein antagonist of K-Ras/B-Raf interaction.
Kauke MJ, Traxlmayr MW, Parker JA, Kiefer JD, Knihtila R, McGee J, Verdine G, Mattos C, Wittrup KD
Sci Rep 7 5831 (2017)
PMID: 28724936

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-134005 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
GTPase KRas, N-terminally processed Chain: A
Molecule details ›
Chain: A
Length: 166 amino acids
Theoretical weight: 18.88 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
R11.1.6 Chain: B
Molecule details ›
Chain: B
Length: 61 amino acids
Theoretical weight: 7.26 KDa
Source organism: Saccharolobus solfataricus
Expression system: Escherichia coli
Structure domains: OB fold (Dihydrolipoamide Acetyltransferase, E2P)

Ligands and Environments

6 bound ligands:
Ligand GNP 1 x GNP
Ligand CA 3 x CA
Ligand CD 4 x CD
Ligand CL 3 x CL
Ligand MG 1 x MG
Ligand CO 3 x CO
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU MICROMAX-007 HF
Spacegroup: P212121
Unit cell:
a: 48.713Å b: 64.648Å c: 74.506Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.19 0.184 0.241
Expression system: Escherichia coli

Quick links

Citations

13 review citations

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

4 mentions without citation

The K-Ras, N-Ras, and H-Ras Isoforms: Unique Conformational Preferences and Implications for Targeting Oncogenic Mutants.
Parker et al. (2018)
3 more