› 3uay

X-ray diffraction
1.4Å resolution

Crystal structure of Bacillus cereus adenosine phosphorylase D204N mutant complexed with adenosine

Released:
DOI: 10.2210/pdb3uay/pdb
PDB entry 3uay coloured by chain, front view.
PDB entry 3uay coloured by chain, side view.
PDB entry 3uay coloured by chain, top view.
Source organism: Bacillus cereus
Primary publication:
Structural basis of the substrate specificity of Bacillus cereus adenosine phosphorylase.
Dessanti P, Zhang Y, Allegrini S, Tozzi MG, Sgarrella F, Ealick SE
Acta Crystallogr D Biol Crystallogr 68 239-48 (2012)
PMID: 22349225

Function and Biology Details

Reaction catalysed: 
Purine deoxynucleoside + phosphate = purine + 2'-deoxy-alpha-D-ribose 1-phosphate
Biochemical function:
Biological process:
Cellular component:
Sequence domains:

Structure analysis Details

Assembly composition:
homo hexamer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-177017 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Purine nucleoside phosphorylase DeoD-type Chain: A
Molecule details ›
Chain: A
Length: 235 amino acids
Theoretical weight: 25.7 KDa
Source organism: Bacillus cereus
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: Q5EEL8 (Residues: 1-235; Coverage: 100%)
Gene name: deoD
Sequence domains: Phosphorylase superfamily
Structure domains: Nucleoside phosphorylase domain

Ligands and Environments

3 bound ligands:
Ligand ADN 1 x ADN
Ligand SO4 1 x SO4
Ligand GOL 2 x GOL
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 24-ID-C
Spacegroup: P6322
Unit cell:
a: 122.2Å b: 122.2Å c: 68.2Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.138 0.137 0.152
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

7 citation in other articles

Recombinant purine nucleoside phosphorylases from thermophiles: preparation, properties and activity towards purine and pyrimidine nucleosides.
Zhou et al. (2013)
6 more

3 mentions without citation

Strained Conformations of Nucleosides in Active Sites of Nucleoside Phosphorylases.
Il'icheva et al. (2020)
2 more