2oec

X-ray diffraction
2.19Å resolution

Crystal structure of the uridine phosphorylase from Salmonella typhimurium in complex with 2,2'-anhydrouridine and potassium ion at 2.194A resolution

Released:
Entry authors: Timofeev VI, Lashkov AA, Pavlyuk BP, Mikhailov AM

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
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: 27.04 KDa
Source organism: Salmonella enterica subsp. enterica serovar Typhimurium str. LT2
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: P0A1F6 (Residues: 2-253; Coverage: 100%)
Gene names: STM3968, STMD1.21, udp
Sequence domains: Phosphorylase superfamily
Structure domains: Nucleoside phosphorylase domain

Ligands and Environments

No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: EMBL/DESY, HAMBURG BEAMLINE X13
Spacegroup: P212121
Unit cell:
a: 88.52Å b: 123.98Å c: 133.52Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.178 0.178 0.24
Expression system: Escherichia coli BL21(DE3)