› 3m8w

X-ray diffraction
1.85Å resolution

Function and Biology Details

Reaction catalysed: 
Alpha-D-ribose 1-phosphate = D-ribose 5-phosphate
Biochemical function:
Biological process:
Cellular component:
Sequence domains:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-182450 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Phosphopentomutase Chains: A, B, C
Molecule details ›
Chains: A, B, C
Length: 399 amino acids
Theoretical weight: 44.59 KDa
Source organism: Bacillus cereus ATCC 14579
Expression system: Escherichia coli BL21
UniProt:
  • Canonical: Q818Z9 (Residues: 2-394; Coverage: 100%)
Gene names: BC_4087, deoB
Sequence domains: Metalloenzyme superfamily
Structure domains:

Ligands and Environments

3 bound ligands:
Ligand MN 10 x MN
Ligand TRS 2 x TRS
Ligand ACT 3 x ACT
1 modified residue:
Ligand TPO 3 x TPO

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 21-ID-G
Spacegroup: P21
Unit cell:
a: 91.238Å b: 76.552Å c: 106.561Å
α: 90° β: 108.89° γ: 90°
R-values:
R R work R free
0.158 0.157 0.186
Expression system: Escherichia coli BL21

Quick links

Citations

2 review citations

Divergence and convergence in enzyme evolution.
Galperin et al. (2012)
1 more

5 mentions without citation

Bioretrosynthetic construction of a didanosine biosynthetic pathway.
Birmingham et al. (2014)
4 more