› 1pr0

X-ray diffraction
2.2Å resolution

Escherichia coli Purine Nucleoside Phosphorylase Complexed with Inosine and Phosphate/Sulfate

Released:
DOI: 10.2210/pdb1pr0/pdb
PDB entry 1pr0 coloured by chain, front view.
PDB entry 1pr0 coloured by chain, side view.
PDB entry 1pr0 coloured by chain, top view.
Source organism: Escherichia coli O157:H7
Primary publication:
Structural basis for substrate specificity of Escherichia coli purine nucleoside phosphorylase.
Bennett EM, Li C, Allan PW, Parker WB, Ealick SE
J Biol Chem 278 47110-8 (2003)
PMID: 12937174

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-142187 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Purine nucleoside phosphorylase DeoD-type Chains: A, B, C
Molecule details ›
Chains: A, B, C
Length: 239 amino acids
Theoretical weight: 25.98 KDa
Source organism: Escherichia coli O157:H7
UniProt:
  • Canonical: P0ABP9 (Residues: 1-239; Coverage: 100%)
Gene names: ECs5343, Z5986, deoD
Sequence domains: Phosphorylase superfamily
Structure domains: Nucleoside phosphorylase domain

Ligands and Environments

2 bound ligands:
Ligand PO4 3 x PO4
Ligand NOS 3 x NOS
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: CHESS BEAMLINE F1
Spacegroup: P6122
Unit cell:
a: 121.2Å b: 121.2Å c: 241.3Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.217 0.215 0.252

Quick links

Citations

7 review citations

Purine-Metabolising Enzymes and Apoptosis in Cancer.
Camici et al. (2019)
6 more

1 mention without citation

The crystal structure of Streptococcus pyogenes uridine phosphorylase reveals a distinct subfamily of nucleoside phosphorylases.
Tran et al. (2011)