X-ray diffraction
2.8Å resolution

Crystal structure of RAC1 F28L mutant

Source organism: Homo sapiens
Primary publication:
RAC1P29S is a spontaneously activating cancer-associated GTPase.
Proc. Natl. Acad. Sci. U.S.A. (2013)
PMID: 23284172

Function and Biology Details

Structure analysis Details

Assembly composition:
monomeric (preferred)
Entry contents:
1 distinct polypeptide molecule
Ras-related C3 botulinum toxin substrate 1 Chains: A, B
Molecule details ›
Chains: A, B
Length: 204 amino acids
Theoretical weight: 22.7 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21(DE3)
  • Canonical: P63000 (Residues: 2-177; Coverage: 92%)
Gene names: MIG5, RAC1, TC25
Structure domains: P-loop containing nucleotide triphosphate hydrolases

Ligands and Environments

2 bound ligands:

No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 24-ID-C
Spacegroup: P21
Unit cell:
a: 40.094Å b: 98.807Å c: 51.994Å
α: 90° β: 90.21° γ: 90°
R R work R free
0.255 0.254 0.288
Expression system: Escherichia coli BL21(DE3)