1u1e

X-ray diffraction
2Å resolution

Structure of e. coli uridine phosphorylase complexed to 5(phenylseleno)acyclouridine (PSAU)

Released:
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)
Assembly name:
PDBe Complex ID:
PDB-CPX-146313 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
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
UniProt:
  • Canonical: P12758 (Residues: 2-253; Coverage: 100%)
Gene names: JW3808, b3831, udp
Sequence domains: Phosphorylase superfamily
Structure domains: Nucleoside phosphorylase domain

Ligands and Environments

3 bound ligands:
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 8-BM
Spacegroup: P212121
Unit cell:
a: 91.076Å b: 125.69Å c: 140.899Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.214 0.211 0.235
Expression system: Escherichia coli