› 6p0z

X-ray diffraction
1.01Å resolution

Crystal structure of N-acetylated KRAS (2-169) bound to GDP and Mg

Released:
DOI: 10.2210/pdb6p0z/pdb
Model geometry
Data not analysed
Fit model/data
Data not analysed
PDB entry 6p0z coloured by chain, front view.
PDB entry 6p0z coloured by chain, side view.
PDB entry 6p0z 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
OpenAccess logo 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)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
GTPase KRas, N-terminally processed Chains: A, B
Molecule details ›
Chains: A, B
Length: 168 amino acids
Theoretical weight: 19.14 KDa
Source organism: Homo sapiens
Expression system: unidentified baculovirus
UniProt:
  • Canonical: P01116 (Residues: 2-169; Coverage: 89%)
  • Best match: P01116-2 (Residues: 2-169)
Gene names: KRAS, KRAS2, RASK2
Sequence domains: Ras family

Ligands and Environments

4 bound ligands:
Ligand MG 2 x MG
Ligand GDP 2 x GDP
Ligand ACE 2 x ACE
Ligand PEG 1 x PEG
No modified residues

Experiments and Validation Details

wwPDB Validation report is not available for this entry.
X-ray source: APS BEAMLINE 24-ID-E
Spacegroup: C2
Unit cell:
a: 65.194Å b: 41.571Å c: 115.41Å
α: 90° β: 104.59° γ: 90°
R-values:
R R work R free
0.145 0.144 0.166
Expression system: unidentified baculovirus

Quick links

Citations

7 review citations

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

5 mentions without citation

Structures of N-terminally processed KRAS provide insight into the role of N-acetylation.
Dharmaiah et al. (2019)
4 more