› 3tkb

X-ray diffraction
1.5Å resolution

crystal structure of human uracil-DNA glycosylase D183G/K302R mutant

Released:
DOI: 10.2210/pdb3tkb/pdb
PDB entry 3tkb coloured by chain, front view.
PDB entry 3tkb coloured by chain, side view.
PDB entry 3tkb coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Thermal unfolding studies of cold adapted uracil-DNA N-glycosylase (UNG) from Atlantic cod (Gadus morhua). A comparative study with human UNG.
Assefa NG, Niiranen L, Willassen NP, Smalås A, Moe E
Comp Biochem Physiol B Biochem Mol Biol 161 60-8 (2012)
PMID: 21959147

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 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: 25.51 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

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

Experiments and Validation Details

Entry percentile scores
X-ray source: BESSY BEAMLINE 14.2
Spacegroup: P21
Unit cell:
a: 42.53Å b: 39.71Å c: 66.73Å
α: 90° β: 97.91° γ: 90°
R-values:
R R work R free
0.154 0.152 0.192
Expression system: Escherichia coli

Quick links

Citations

6 citation in other articles

Computer simulations explain the anomalous temperature optimum in a cold-adapted enzyme.
Sočan et al. (2020)
5 more

1 mention without citation

Structural Aspects of DNA Repair and Recombination in Crop Improvement.
Verma et al. (2020)