› 1rxc

X-ray diffraction
2.35Å resolution

Function and Biology Details

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

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, G, H, I, J, K, L
Molecule details ›
Chains: A, B, C, D, E, F, G, H, I, J, K, L
Length: 253 amino acids
Theoretical weight: 27.19 KDa
Source organism: Escherichia coli
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: P12758 (Residues: 1-253; Coverage: 100%)
Gene names: JW3808, b3831, udp
Sequence domains: Phosphorylase superfamily
Structure domains: Nucleoside phosphorylase domain

Ligands and Environments

5 bound ligands:
Ligand K 5 x K
Ligand R1P 8 x R1P
Ligand URF 8 x URF
Ligand PO4 1 x PO4
Ligand 5UD 1 x 5UD
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU RU200H
Spacegroup: P21
Unit cell:
a: 90.188Å b: 191.701Å c: 91.909Å
α: 90° β: 118.5° γ: 90°
R-values:
R R work R free
0.153 0.15 0.202
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

2 review citations

Role of Na+ and K+ in enzyme function.
Page et al. (2006)
1 more

3 mentions without citation

The crystal structure and activity of a putative trypanosomal nucleoside phosphorylase reveal it to be a homodimeric uridine phosphorylase.
Larson et al. (2010)
2 more