› 5wha

X-ray diffraction
2.04Å resolution

KRas G12V, bound to GDP and miniprotein 225-11

Released:
DOI: 10.2210/pdb5wha/pdb
PDB entry 5wha coloured by chain, front view.
PDB entry 5wha coloured by chain, side view.
PDB entry 5wha 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-134007 (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: 19.15 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 MG 4 x MG
Ligand GDP 4 x GDP
Ligand CA 8 x CA
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 24-ID-E
Spacegroup: P21
Unit cell:
a: 48.003Å b: 40.328Å c: 230.939Å
α: 90° β: 90.99° γ: 90°
R-values:
R R work R free
0.24 0.238 0.277
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