› 1o4v

X-ray diffraction
1.77Å resolution

Function and Biology Details

Reaction catalysed: 
5-carboxyamino-1-(5-phospho-D-ribosyl)imidazole = 5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxylate
Biochemical function:
Biological process:
Cellular component:
  • not assigned
Sequence domains:
Structure domain:

Structure analysis Details

Assembly composition:
homo octamer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-194542 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
N5-carboxyaminoimidazole ribonucleotide mutase Chain: A
Molecule details ›
Chain: A
Length: 183 amino acids
Theoretical weight: 20.07 KDa
Source organism: Thermotoga maritima
Expression system: Escherichia coli
UniProt:
  • Canonical: Q9WYS7 (Residues: 2-171; Coverage: 99%)
Gene names: TM_0446, purE
Sequence domains: AIR carboxylase
Structure domains: Rossmann fold

Ligands and Environments

1 bound ligand:
Ligand SO4 2 x SO4
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SSRL BEAMLINE BL11-1
Spacegroup: I422
Unit cell:
a: 103.249Å b: 103.249Å c: 65.445Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.151 0.15 0.182
Expression system: Escherichia coli

Quick links

Citations

1 review citation

Microbial biochemistry, physiology, and biotechnology of hyperthermophilic Thermotoga species.
Conners et al. (2006)
7 other articles

3 mentions without citation

Improvement of molecular-replacement models with Sculptor.
Bunkóczi et al. (2011)
2 more