› 3un3

X-ray diffraction
1.8Å resolution

phosphopentomutase T85Q variant soaked with glucose 1,6-bisphosphate

Released:
DOI: 10.2210/pdb3un3/pdb
PDB entry 3un3 coloured by chain, front view.
PDB entry 3un3 coloured by chain, side view.
PDB entry 3un3 coloured by chain, top view.
Source organism: Bacillus cereus
Primary publication:
Molecular differences between a mutase and a phosphatase: investigations of the activation step in Bacillus cereus phosphopentomutase.
Iverson TM, Panosian TD, Birmingham WR, Nannemann DP, Bachmann BO
Biochemistry 51 1964-75 (2012)
PMID: 22329805

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: 44.54 KDa
Source organism: Bacillus cereus
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 12 x MN
Ligand GOL 3 x GOL
Ligand G16 2 x G16
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 21-ID-G
Spacegroup: P21
Unit cell:
a: 91.56Å b: 76.781Å c: 106.77Å
α: 90° β: 108.55° γ: 90°
R-values:
R R work R free
0.166 0.164 0.191
Expression system: Escherichia coli BL21

Quick links

Citations

4 citation in other articles

Remote-controlled robotic platform ORPHEUS as a new tool for detection of bacteria in the environment.
Nejdl et al. (2014)
3 more

2 mentions without citation

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