› 1udh

X-ray diffraction
1.75Å resolution

THE STRUCTURAL BASIS OF SPECIFIC BASE EXCISION REPAIR BY URACIL-DNA GLYCOSYLASE

Released:
DOI: 10.2210/pdb1udh/pdb
PDB entry 1udh coloured by chain, front view.
PDB entry 1udh coloured by chain, side view.
PDB entry 1udh coloured by chain, top view.
Source organism: Human alphaherpesvirus 1 strain 17
Primary publication:
The structural basis of specific base-excision repair by uracil-DNA glycosylase.
Savva R, McAuley-Hecht K, Brown T, Pearl L
Nature 373 487-93 (1995)
PMID: 7845459

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
Sequence domains:
Structure domain:

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: 27.37 KDa
Source organism: Human alphaherpesvirus 1 strain 17
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:
Ligand SO4 2 x SO4
Ligand URA 1 x URA
No modified residues

Experiments and Validation Details

Entry percentile scores
Spacegroup: P31
Unit cell:
a: 65.14Å b: 65.14Å c: 49.16Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.191 0.191 0.237

Quick links

Citations

61 review citations

Genome editing with CRISPR-Cas nucleases, base editors, transposases and prime editors.
Anzalone et al. (2020)
60 more

6 mentions without citation

Recent advances in the structural mechanisms of DNA glycosylases.
Brooks et al. (2013)
5 more