› 1lqj

X-ray diffraction
3.35Å 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 domain:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-146128 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Uracil-DNA glycosylase Chains: A, B, C, D
Molecule details ›
Chains: A, B, C, D
Length: 229 amino acids
Theoretical weight: 25.73 KDa
Source organism: Escherichia coli
Expression system: Escherichia coli
UniProt:
  • Canonical: P12295 (Residues: 2-229; Coverage: 100%)
Gene names: JW2564, b2580, ung
Sequence domains: Uracil DNA glycosylase superfamily
Structure domains: Uracil-DNA glycosylase-like domain

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU RU200
Spacegroup: P32
Unit cell:
a: 125.21Å b: 125.21Å c: 90.047Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.241 0.241 0.326
Expression system: Escherichia coli

Quick links

Citations

3 review citations

A Decade of Biochemical and Structural Studies of the DNA Repair Machinery of Deinococcus radiodurans: Major Findings, Functional and Mechanistic Insight and Challenges.
Timmins et al. (2016)
2 more