› 1o1x

X-ray diffraction
1.9Å resolution

Function and Biology Details

Reaction catalysed: 
D-ribose 5-phosphate = D-ribulose 5-phosphate
Biochemical function:
Biological process:
Cellular component:
  • not assigned
Sequence domains:
Structure domain:

Structure analysis Details

Assembly composition:
homo tetramer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-194713 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Sugar-phosphate isomerase Chain: A
Molecule details ›
Chain: A
Length: 155 amino acids
Theoretical weight: 17.51 KDa
Source organism: Thermotoga maritima
Expression system: Escherichia coli
UniProt:
  • Canonical: Q9X0G9 (Residues: 2-143; Coverage: 99%)
Gene name: TM_1080
Sequence domains: Ribose/Galactose Isomerase
Structure domains: Sugar-phosphate isomerase, RpiB/LacA/LacB

Ligands and Environments

1 bound ligand:
Ligand MPD 1 x MPD
2 modified residues:
Ligand MSE 3 x MSE
Ligand OCS 1 x OCS

Experiments and Validation Details

Entry percentile scores
X-ray source: SSRL BEAMLINE BL9-1
Spacegroup: I222
Unit cell:
a: 61.49Å b: 73.89Å c: 87.74Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.118 0.117 0.138
Expression system: Escherichia coli

Quick links

Citations

1 review citation

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

4 mentions without citation

Decision-making in structure solution using Bayesian estimates of map quality: the PHENIX AutoSol wizard.
Terwilliger et al. (2009)
3 more