› 1qe5

X-ray diffraction
2.2Å resolution

PURINE NUCLEOSIDE PHOSPHORYLASE FROM CELLULOMONAS SP. IN COMPLEX WITH PHOSPHATE

Released:
DOI: 10.2210/pdb1qe5/pdb
PDB entry 1qe5 coloured by chain, front view.
PDB entry 1qe5 coloured by chain, side view.
PDB entry 1qe5 coloured by chain, top view.
Source organism: Cellulomonas sp.
Primary publication:
Crystal structure of the purine nucleoside phosphorylase (PNP) from Cellulomonas sp. and its implication for the mechanism of trimeric PNPs.
Tebbe J, Bzowska A, Wielgus-Kutrowska B, Schröder W, Kazimierczuk Z, Shugar D, Saenger W, Koellner G
J Mol Biol 294 1239-55 (1999)
PMID: 10600382

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 trimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-160596 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Purine nucleoside phosphorylase Chains: A, B, C
Molecule details ›
Chains: A, B, C
Length: 266 amino acids
Theoretical weight: 27.55 KDa
Source organism: Cellulomonas sp.
UniProt:
  • Canonical: P81989 (Residues: 9-282; Coverage: 94%)
Gene name: punA
Sequence domains: Phosphorylase superfamily
Structure domains: Nucleoside phosphorylase domain

Ligands and Environments

2 bound ligands:
Ligand PO4 3 x PO4
Ligand CA 1 x CA
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: EMBL/DESY, HAMBURG BEAMLINE X11
Spacegroup: P212121
Unit cell:
a: 64.12Å b: 108.9Å c: 119.3Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.2 0.2 0.26

Quick links

Citations

6 review citations

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