› 2j8x

X-ray diffraction
2.3Å resolution

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:
Sequence domains:
Structure domains:

Structure analysis Details

Assembly composition:
hetero dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-146367 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Uracil-DNA glycosylase Chains: A, C
Molecule details ›
Chains: A, C
Length: 231 amino acids
Theoretical weight: 25.76 KDa
Source organism: human gammaherpesvirus 4
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: P12888 (Residues: 25-255; Coverage: 91%)
Gene names: BKRF3, UNG
Sequence domains: Uracil DNA glycosylase superfamily
Structure domains: Uracil-DNA glycosylase-like domain
Uracil-DNA glycosylase inhibitor Chains: B, D
Molecule details ›
Chains: B, D
Length: 84 amino acids
Theoretical weight: 9.48 KDa
Source organism: Bacillus phage PBS2
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: P14739 (Residues: 1-84; Coverage: 100%)
Gene name: UGI
Sequence domains: Uracil-DNA glycosylase inhibitor
Structure domains: Bacteriophage PBS2, uracil-glycosylase inhibitor

Ligands and Environments

1 bound ligand:
Ligand URE 2 x URE
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE ID14-1
Spacegroup: C2221
Unit cell:
a: 62.406Å b: 82.942Å c: 269.13Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.196 0.193 0.257
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

1 review citation

Uracil-DNA glycosylase: Structural, thermodynamic and kinetic aspects of lesion search and recognition.
Zharkov et al. (2010)
12 other articles

5 mentions without citation

The Essential Co-Option of Uracil-DNA Glycosylases by Herpesviruses Invites Novel Antiviral Design.
Savva R. (2020)
4 more