2atv

X-ray diffraction
1.9Å resolution

The crystal structure of human RERG in the GDP bound state

Released:
Source organism: Homo sapiens
Entry authors: Turnbull AP, Salah E, Schoch G, Elkins J, Burgess N, Gileadi O, von Delft F, Weigelt J, Edwards A, Arrowsmith C, Sundstrom M, Doyle D, Structural Genomics Consortium (SGC)

Function and Biology Details

Reaction catalysed:
GTP + H(2)O = GDP + phosphate
Biochemical function:
Biological process:
  • not assigned
Cellular component:
  • not assigned

Structure analysis Details

Assembly composition:
monomeric (preferred)
PDBe Complex ID:
PDB-CPX-188351 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Ras-related and estrogen-regulated growth inhibitor Chain: A
Molecule details ›
Chain: A
Length: 196 amino acids
Theoretical weight: 22.38 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: Q96A58 (Residues: 1-174; Coverage: 87%)
Gene name: RERG
Sequence domains: Ras family
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: SLS BEAMLINE X10SA
Spacegroup: P41212
Unit cell:
a: 76.405Å b: 76.405Å c: 107.876Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.206 0.204 0.234
Expression system: Escherichia coli