› 2c56

X-ray diffraction
2.1Å resolution

A comparative study of uracil DNA glycosylases from human and herpes simplex virus type 1

Released:
DOI: 10.2210/pdb2c56/pdb
PDB entry 2c56 coloured by chain, front view.
PDB entry 2c56 coloured by chain, side view.
PDB entry 2c56 coloured by chain, top view.
Source organism: Human alphaherpesvirus 1
Primary publication:
A comparative study of uracil-DNA glycosylases from human and herpes simplex virus type 1.
Krusong K, Carpenter EP, Bellamy SR, Savva R, Baldwin GS
J Biol Chem 281 4983-92 (2006)
PMID: 16306042

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-145198 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecules (2 distinct):
Uracil-DNA glycosylase Chain: A
Molecule details ›
Chain: A
Length: 244 amino acids
Theoretical weight: 27.34 KDa
Source organism: Human alphaherpesvirus 1
Expression system: Escherichia coli BL21
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

Carbohydrate polymer : NEW Components: GLC, FRU
Carbohydrate polymer
No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SRS BEAMLINE PX9.6
Spacegroup: P21
Unit cell:
a: 42.04Å b: 61.117Å c: 43.392Å
α: 90° β: 92.25° γ: 90°
R-values:
R R work R free
0.151 0.151 0.212
Expression system: Escherichia coli BL21

Quick links

Citations

3 review citations

Uracil-DNA glycosylases-structural and functional perspectives on an essential family of DNA repair enzymes.
Schormann et al. (2014)
2 more