› 5lu0

X-ray diffraction
1.73Å resolution

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-157474 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Purine nucleoside phosphorylase DeoD-type Chains: A, B, C, D, E, F
Molecule details ›
Chains: A, B, C, D, E, F
Length: 233 amino acids
Theoretical weight: 25.82 KDa
Source organism: Helicobacter pylori
UniProt:
  • Canonical: P56463 (Residues: 1-233; Coverage: 100%)
Gene names: HP_1178, deoD
Sequence domains: Phosphorylase superfamily
Structure domains: Nucleoside phosphorylase domain

Ligands and Environments

3 bound ligands:
Ligand PO4 4 x PO4
Ligand TRS 4 x TRS
Ligand EDO 10 x EDO
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ELETTRA BEAMLINE 5.2R
Spacegroup: P212121
Unit cell:
a: 59.52Å b: 86.31Å c: 268.449Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.186 0.184 0.228

Quick links

Citations

2 review citations

Helicobacter pylori treatment in the post-antibiotics era-searching for new drug targets.
Roszczenko-Jasińska et al. (2020)
1 more

2 mentions without citation

Helicobacter pylori purine nucleoside phosphorylase shows new distribution patterns of open and closed active site conformations and unusual biochemical features.
Narczyk et al. (2018)
1 more