› 3euf

X-ray diffraction
1.9Å resolution

Crystal structure of BAU-bound human uridine phosphorylase 1

Released:
DOI: 10.2210/pdb3euf/pdb
PDB entry 3euf coloured by chain, front view.
PDB entry 3euf coloured by chain, side view.
PDB entry 3euf coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Implications of the structure of human uridine phosphorylase 1 on the development of novel inhibitors for improving the therapeutic window of fluoropyrimidine chemotherapy.
Roosild TP, Castronovo S, Fabbiani M, Pizzorno G
BMC Struct Biol 9 14 (2009)
PMID: 19291308

Function and Biology Details

Reaction catalysed: 
Uridine + phosphate = uracil + alpha-D-ribose 1-phosphate
Biochemical function:
Biological process:
Cellular component:
Sequence domains:

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-172590 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Uridine phosphorylase 1 Chains: A, B, C, D
Molecule details ›
Chains: A, B, C, D
Length: 328 amino acids
Theoretical weight: 36.05 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: Q16831 (Residues: 1-310; Coverage: 100%)
Gene names: UP, UPP1
Sequence domains: Phosphorylase superfamily
Structure domains: Nucleoside phosphorylase domain

Ligands and Environments

2 bound ligands:
Ligand BAU 4 x BAU
Ligand PO4 4 x PO4
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SSRL BEAMLINE BL7-1
Spacegroup: P212121
Unit cell:
a: 66.197Å b: 74.442Å c: 262.707Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.205 0.202 0.251
Expression system: Escherichia coli

Quick links

Citations

1 review citation

Modulators of nucleoside metabolism in the therapy of brain diseases.
Boison D. (2011)
9 other articles

7 mentions without citation

Proteome-wide covalent ligand discovery in native biological systems.
Backus et al. (2016)
6 more