› 5whd

X-ray diffraction
1.64Å resolution

Crystal structure of KRas G12V/D38P, bound to GDP

Released:
DOI: 10.2210/pdb5whd/pdb
PDB entry 5whd coloured by chain, front view.
PDB entry 5whd coloured by chain, side view.
PDB entry 5whd coloured by chain, top view.
Source organism: Homo sapiens
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

Assemblies composition:
monomeric (preferred)
homo dimer
Assembly name:
PDBe Complex ID:
PDB-CPX-133991 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
GTPase KRas, N-terminally processed Chains: A, B, C, D
Molecule details ›
Chains: A, B, C, D
Length: 170 amino acids
Theoretical weight: 19.14 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

Ligands and Environments

1 bound ligand:
Ligand GDP 4 x GDP
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 24-ID-E
Spacegroup: P21
Unit cell:
a: 37.239Å b: 80.912Å c: 108.041Å
α: 90° β: 90.62° γ: 90°
R-values:
R R work R free
0.194 0.192 0.225
Expression system: Escherichia coli

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