2ic5

X-ray diffraction
1.9Å resolution

Crystal structure of human RAC3 grown in the presence of Gpp(NH)p.

Released:
Source organism: Homo sapiens
Entry authors: Ugochukwu E, Yang X, Zao Y, Elkins J, Gileadi C, Burgess N, Colebrook S, Gileadi O, Fedorov O, Bunkoczi G, Sundstrom M, Arrowsmith C, Weigelt J, Edwards A, von Delft F, Doyle D, Structural Genomics Consortium (SGC)

Function and Biology Details

Reaction catalysed:
GTP + H(2)O = GDP + phosphate
Biochemical function:
Cellular component:

Structure analysis Details

Assembly composition:
monomeric (preferred)
PDBe Complex ID:
PDB-CPX-158088 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Ras-related C3 botulinum toxin substrate 3 Chains: A, B
Molecule details ›
Chains: A, B
Length: 180 amino acids
Theoretical weight: 19.99 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: P60763 (Residues: 1-178; Coverage: 93%)
Gene name: RAC3
Sequence domains: Ras family
Structure domains: P-loop containing nucleotide triphosphate hydrolases

Ligands and Environments

No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SLS BEAMLINE X10SA
Spacegroup: P212121
Unit cell:
a: 53.755Å b: 81.583Å c: 84.381Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.155 0.153 0.2
Expression system: Escherichia coli