4r2x

X-ray diffraction
0.93Å resolution

Unique conformation of uridine and asymmetry of the hexameric molecule revealed in the high-resolution structures of Shewanella oneidensis uridine phosphorylase in the free form and in complex with uridine

Released:
Model geometry
Fit model/data

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-184329 (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: 252 amino acids
Theoretical weight: 26.88 KDa
Source organism: Shewanella oneidensis MR-1
Expression system: Escherichia coli
UniProt:
  • Canonical: Q8E9X9 (Residues: 1-252; Coverage: 100%)
Gene names: SO_4133, udp
Sequence domains: Phosphorylase superfamily
Structure domains: Nucleoside phosphorylase domain

Ligands and Environments

3 bound ligands:
No modified residues

Experiments and Validation Details

wwPDB Validation report is not available for this entry.
X-ray source: SPRING-8 BEAMLINE BL24XU
Spacegroup: P21
Unit cell:
a: 91.54Å b: 95.93Å c: 91.61Å
α: 90° β: 120° γ: 90°
R-values:
R R work R free
0.15 0.149 0.164
Expression system: Escherichia coli