2c53

X-ray diffraction
1.8Å resolution

A comparative study of uracil DNA glycosylases from human and herpes simplex virus type 1

Released:

Function and Biology Details

Reaction catalysed:
Hydrolyzes single-stranded DNA or mismatched double-stranded DNA and polynucleotides, releasing free uracil
Biochemical function:
Biological process:
Cellular component:
  • not assigned

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-145198 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Uracil-DNA glycosylase Chain: A
Molecule details ›
Chain: A
Length: 244 amino acids
Theoretical weight: 27.34 KDa
Source organism: Human alphaherpesvirus 1
Expression system: Escherichia coli BL21
UniProt:
  • Canonical: P10186 (Residues: 91-334; Coverage: 73%)
Gene name: UL2
Sequence domains: Uracil DNA glycosylase superfamily
Structure domains: Uracil-DNA glycosylase-like domain

Ligands and Environments

2 bound ligands:
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SRS BEAMLINE PX9.6
Spacegroup: P21
Unit cell:
a: 42.406Å b: 61.161Å c: 43.62Å
α: 90° β: 93.15° γ: 90°
R-values:
R R work R free
0.164 0.164 0.216
Expression system: Escherichia coli BL21