PDBe 1rfg

X-ray diffraction
2.9Å resolution

Crystal Structure of Human Purine Nucleoside Phosphorylase Complexed with Guanosine

Released:
Source organism: Homo sapiens
Primary publication:
Structure of human PNP complexed with ligands.
Acta Crystallogr. D Biol. Crystallogr. 61 856-62 (2005)
PMID: 15983407

Function and Biology Details

Reaction catalysed:
(1) Purine nucleoside + phosphate = purine + alpha-D-ribose 1-phosphate. (2) Purine deoxynucleoside + phosphate = purine + 2'-deoxy-alpha-D-ribose 1-phosphate. 
Biochemical function:
Biological process:
Cellular component:

Structure analysis Details

Assembly composition:
homo trimer (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Purine nucleoside phosphorylase Chain: E
Molecule details ›
Chain: E
Length: 288 amino acids
Theoretical weight: 32.05 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: P00491 (Residues: 2-289; Coverage: 100%)
Gene names: NP, PNP
Sequence domains: Phosphorylase superfamily
Structure domains: Rossmann fold

Ligands and Environments

2 bound ligands:

No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: LNLS BEAMLINE D03B-MX1
Spacegroup: R32
Unit cell:
a: 139.38Å b: 139.38Å c: 160.4Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.206 0.206 0.267
Expression system: Escherichia coli