› 1ula

X-ray diffraction
2.75Å resolution

APPLICATION OF CRYSTALLOGRAPHIC AND MODELING METHODS IN THE DESIGN OF PURINE NUCLEOSIDE PHOSPHORYLASE INHIBITORS

Released:
DOI: 10.2210/pdb1ula/pdb
PDB entry 1ula coloured by chain, front view.
PDB entry 1ula coloured by chain, side view.
PDB entry 1ula coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Application of crystallographic and modeling methods in the design of purine nucleoside phosphorylase inhibitors.
Ealick SE, Babu YS, Bugg CE, Erion MD, Guida WC, Montgomery JA, Secrist JA
Proc Natl Acad Sci U S A 88 11540-4 (1991)
PMID: 1763067

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-132560 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Purine nucleoside phosphorylase Chain: A
Molecule details ›
Chain: A
Length: 289 amino acids
Theoretical weight: 32.18 KDa
Source organism: Homo sapiens
Expression system: Not provided
UniProt:
  • Canonical: P00491 (Residues: 1-289; Coverage: 100%)
Gene names: NP, PNP
Sequence domains: Phosphorylase superfamily
Structure domains: Nucleoside phosphorylase domain

Ligands and Environments

1 bound ligand:
Ligand SO4 2 x SO4
No modified residues

Experiments and Validation Details

Entry percentile scores
Spacegroup: R32
Unit cell:
a: 142.9Å b: 142.9Å c: 165.2Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.202 not available not available
Expression system: Not provided

Quick links

Citations

12 review citations

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

10 mentions without citation

LIGSITEcsc: predicting ligand binding sites using the Connolly surface and degree of conservation.
Huang et al. (2006)
9 more