X-ray diffraction
1.95Å resolution

Structure of E. coli uridine phosphorylase complexed to 5-(m-(benzyloxy)benzyl)barbituric acid (BBBA)

Source organism: Escherichia coli
Primary publication:
Structural basis for inhibition of Escherichia coli uridine phosphorylase by 5-substituted acyclouridines.
Acta Crystallogr. D Biol. Crystallogr. 61 863-72 (2005)
PMID: 15983408

Function and Biology Details

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

Structure analysis Details

Assembly composition:
homo hexamer (preferred)
Entry contents:
1 distinct polypeptide molecule
Uridine phosphorylase Chains: A, B, C, D, E, F
Molecule details ›
Chains: A, B, C, D, E, F
Length: 256 amino acids
Theoretical weight: 27.47 KDa
Source organism: Escherichia coli
Expression system: Escherichia coli
  • Canonical: P12758 (Residues: 2-253; Coverage: 100%)
Gene names: JW3808, b3831, udp
Sequence domains: Phosphorylase superfamily
Structure domains: Nucleoside phosphorylase domain

Ligands and Environments

2 bound ligands:
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 8-BM
Spacegroup: P212121
Unit cell:
a: 92.677Å b: 127.124Å c: 143.355Å
α: 90° β: 90° γ: 90°
R R work R free
0.201 0.2 0.221
Expression system: Escherichia coli