› 5whe

X-ray diffraction
1.91Å resolution

KRas G12V/D38P, bound to GppNHp and miniprotein 225-11

Released:
DOI: 10.2210/pdb5whe/pdb
PDB entry 5whe coloured by chain, front view.
PDB entry 5whe coloured by chain, side view.
PDB entry 5whe 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-134009 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
GTPase KRas, N-terminally processed Chains: A, D, G, J
Molecule details ›
Chains: A, D, G, J
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
Miniprotein 225-11 Chains: B, C, E, F, H, I, K, L
Molecule details ›
Chains: B, C, E, F, H, I, K, L
Length: 35 amino acids
Theoretical weight: 4 KDa
Source organism: synthetic construct
Expression system: Escherichia coli

Ligands and Environments

3 bound ligands:
Ligand GNP 4 x GNP
Ligand CA 10 x CA
Ligand MG 4 x MG
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 24-ID-E
Spacegroup: P21
Unit cell:
a: 40.549Å b: 232.525Å c: 48.213Å
α: 90° β: 90.16° γ: 90°
R-values:
R R work R free
0.187 0.184 0.227
Expression system: Escherichia coli

Quick links

Citations

9 review citations

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

3 mentions without citation

RAS Nanoclusters: Dynamic Signaling Platforms Amenable to Therapeutic Intervention.
Van et al. (2021)
2 more