› 2ai1

X-ray diffraction
2Å resolution

Purine nucleoside phosphorylase from calf spleen

Released:
DOI: 10.2210/pdb2ai1/pdb
PDB entry 2ai1 coloured by chain, front view.
PDB entry 2ai1 coloured by chain, side view.
PDB entry 2ai1 coloured by chain, top view.
Source organism: Bos taurus
Primary publication:
Novel multisubstrate inhibitors of mammalian purine nucleoside phosphorylase.
Toms AV, Wang W, Li Y, Ganem B, Ealick SE
Acta Crystallogr D Biol Crystallogr 61 1449-58 (2005)
PMID: 16239721

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-157333 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Purine nucleoside phosphorylase Chain: A
Molecule details ›
Chain: A
Length: 289 amino acids
Theoretical weight: 32.13 KDa
Source organism: Bos taurus
UniProt:
  • Canonical: P55859 (Residues: 1-289; Coverage: 100%)
Gene names: NP, PNP
Sequence domains: Phosphorylase superfamily
Structure domains: Nucleoside phosphorylase domain

Ligands and Environments

4 bound ligands:
Ligand MG 1 x MG
Ligand ZN 1 x ZN
Ligand 144 1 x 144
Ligand P1G 1 x P1G
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: CHESS BEAMLINE F1
Spacegroup: P213
Unit cell:
a: 93.952Å b: 93.952Å c: 93.952Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.214 0.212 0.254

Quick links

Citations

1 review citation

Computational methods for de novo protein design and its applications to the human immunodeficiency virus 1, purine nucleoside phosphorylase, ubiquitin specific protease 7, and histone demethylases.
Bellows et al. (2010)
3 other articles

1 mention without citation

Why Purine Nucleoside Phosphorylase Ribosylates 2,6-Diamino-8-azapurine in Noncanonical Positions? A Molecular Modeling Study.
Pyrka et al. (2020)