› 6mbt

X-ray diffraction
1.45Å resolution

Crystal structure of wild-type KRAS bound to GDP and Mg (Space group C2)

Released:
DOI: 10.2210/pdb6mbt/pdb
PDB entry 6mbt coloured by chain, front view.
PDB entry 6mbt coloured by chain, side view.
PDB entry 6mbt coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Structures of N-terminally processed KRAS provide insight into the role of N-acetylation.
Dharmaiah S, Tran TH, Messing S, Agamasu C, Gillette WK, Yan W, Waybright T, Alexander P, Esposito D, Nissley DV, McCormick F, Stephen AG, Simanshu DK
Sci Rep 9 10512 (2019)
PMID: 31324887

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:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-133991 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
GTPase KRas, N-terminally processed Chains: A, B
Molecule details ›
Chains: A, B
Length: 170 amino acids
Theoretical weight: 19.33 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: P01116 (Residues: 1-169; Coverage: 89%)
Gene names: KRAS, KRAS2, RASK2
Sequence domains: Ras family

Ligands and Environments

2 bound ligands:
Ligand GDP 2 x GDP
Ligand MG 2 x MG
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 24-ID-E
Spacegroup: C2
Unit cell:
a: 66.287Å b: 41.552Å c: 115.38Å
α: 90° β: 105.05° γ: 90°
R-values:
R R work R free
0.178 0.177 0.216
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

5 review citations

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

9 mentions without citation

Recent Updates on the Significance of KRAS Mutations in Colorectal Cancer Biology.
László et al. (2021)
8 more