› 1ecp

X-ray diffraction
2Å 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 domain:

Structure analysis Details

Assembly composition:
homo hexamer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-142186 (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: 238 amino acids
Theoretical weight: 25.85 KDa
Source organism: Escherichia coli K-12
Expression system: Escherichia coli
UniProt:
  • Canonical: P0ABP8 (Residues: 2-239; Coverage: 100%)
Gene names: JW4347, b4384, deoD, pup
Sequence domains: Phosphorylase superfamily
Structure domains: Nucleoside phosphorylase domain

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
Spacegroup: P21
Unit cell:
a: 89.5Å b: 110.6Å c: 74.6Å
α: 90° β: 111.7° γ: 90°
R-values:
R R work R free
0.2 0.2 0.29
Expression system: Escherichia coli

Quick links

Citations

4 review citations

Purine nucleoside phosphorylases: properties, functions, and clinical aspects.
Bzowska et al. (2000)
3 more

6 mentions without citation

Identifying the subproteome of kinetically stable proteins via diagonal 2D SDS/PAGE.
Xia et al. (2007)
5 more