1u1f

X-ray diffraction
2.3Å resolution

Structure of e. coli uridine phosphorylase complexed to 5-(m-(benzyloxy)benzyl)acyclouridine (BBAU)

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: RIGAKU RU200
Spacegroup: P212121
Unit cell:
a: 91.557Å b: 125.813Å c: 141.137Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.201 0.199 0.228
Expression system: Escherichia coli