› 5wpm

X-ray diffraction
1.72Å resolution

KRas G12V, bound to GppNHp and miniprotein 225-11(A30R)

Released:
DOI: 10.2210/pdb5wpm/pdb
PDB entry 5wpm coloured by chain, front view.
PDB entry 5wpm coloured by chain, side view.
PDB entry 5wpm coloured by chain, top view.
Source organisms:
Primary publication:
Exceptionally high-affinity Ras binders that remodel its effector domain.
McGee JH, Shim SY, Lee SJ, Swanson PK, Jiang SY, Durney MA, Verdine GL
J Biol Chem 293 3265-3280 (2018)
PMID: 29282294

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 trimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-134011 (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: 18.93 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
Ras binding peptide Chains: B, C
Molecule details ›
Chains: B, C
Length: 32 amino acids
Theoretical weight: 3.88 KDa
Source organism: Saccharomyces cerevisiae
Expression system: Not provided

Ligands and Environments

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

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 24-ID-C
Spacegroup: P21
Unit cell:
a: 41.934Å b: 37.81Å c: 70.179Å
α: 90° β: 103.38° γ: 90°
R-values:
R R work R free
0.237 0.235 0.285
Expression systems:
  • Escherichia coli
  • Not provided

Quick links

Citations

9 review citations

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

2 mentions without citation

Exceptionally high-affinity Ras binders that remodel its effector domain.
McGee et al. (2018)
1 more