› 4obe

X-ray diffraction
1.24Å resolution

Crystal Structure of GDP-bound Human KRas

Released:
DOI: 10.2210/pdb4obe/pdb
PDB entry 4obe coloured by chain, front view.
PDB entry 4obe coloured by chain, side view.
PDB entry 4obe coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
In situ selectivity profiling and crystal structure of SML-8-73-1, an active site inhibitor of oncogenic K-Ras G12C.
Hunter JC, Gurbani D, Ficarro SB, Carrasco MA, Lim SM, Choi HG, Xie T, Marto JA, Chen Z, Gray NS, Westover KD
Proc Natl Acad Sci U S A 111 8895-900 (2014)
PMID: 24889603

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
Structure domains: P-loop containing nucleotide triphosphate hydrolases

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 19-ID
Spacegroup: C2
Unit cell:
a: 66.147Å b: 42.096Å c: 114.393Å
α: 90° β: 105.32° γ: 90°
R-values:
R R work R free
0.157 0.157 0.169
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

47 review citations

RAS isoforms and mutations in cancer at a glance.
Hobbs et al. (2016)
46 more

68 mentions without citation

Drugging Ras GTPase: a comprehensive mechanistic and signaling structural view.
Lu et al. (2016)
67 more