› 1akz

X-ray diffraction
1.57Å resolution

HUMAN URACIL-DNA GLYCOSYLASE

Released:
DOI: 10.2210/pdb1akz/pdb
PDB entry 1akz coloured by chain, front view.
PDB entry 1akz coloured by chain, side view.
PDB entry 1akz coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Base excision repair initiation revealed by crystal structures and binding kinetics of human uracil-DNA glycosylase with DNA.
Parikh SS, Mol CD, Slupphaug G, Bharati S, Krokan HE, Tainer JA
EMBO J 17 5214-26 (1998)
PMID: 9724657

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-146445 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Uracil-DNA glycosylase Chain: A
Molecule details ›
Chain: A
Length: 223 amino acids
Theoretical weight: 25.54 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: P13051 (Residues: 94-313; Coverage: 70%)
Gene names: DGU, UNG, UNG1, UNG15
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: SSRL BEAMLINE BL7-1
Spacegroup: P212121
Unit cell:
a: 47.76Å b: 55.27Å c: 84.97Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.189 0.189 0.224
Expression system: Escherichia coli

Quick links

Citations

53 review citations

Uracil in DNA--occurrence, consequences and repair.
Krokan et al. (2002)
52 more

35 mentions without citation

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