› 6mbq

X-ray diffraction
1.35Å resolution

Crystal structure of Mg-free wild-type KRAS (2-166) bound to GMPPNP in the state 1 conformation

Released:
DOI: 10.2210/pdb6mbq/pdb
PDB entry 6mbq coloured by chain, front view.
PDB entry 6mbq coloured by chain, side view.
PDB entry 6mbq 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 Chain: A
Molecule details ›
Chain: A
Length: 167 amino acids
Theoretical weight: 18.87 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: P01116 (Residues: 2-166; Coverage: 87%)
Gene names: KRAS, KRAS2, RASK2
Sequence domains: Ras family

Ligands and Environments

3 bound ligands:
Ligand NA 1 x NA
Ligand EDO 1 x EDO
Ligand GNP 1 x GNP
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 21-ID-F
Spacegroup: P212121
Unit cell:
a: 36.02Å b: 37.91Å c: 99.99Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.136 0.134 0.179
Expression system: Escherichia coli BL21(DE3)

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Citations

7 review citations

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

1 mention without citation

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