› 1lqg

X-ray diffraction
2.9Å resolution

ESCHERICHIA COLI URACIL-DNA GLYCOSYLASE COMPLEX WITH URACIL-DNA GLYCOSYLASE INHIBITOR PROTEIN

Released:
DOI: 10.2210/pdb1lqg/pdb
PDB entry 1lqg coloured by chain, front view.
PDB entry 1lqg coloured by chain, side view.
PDB entry 1lqg coloured by chain, top view.
Source organisms:
Primary publication:
Domain closure and action of uracil DNA glycosylase (UDG): structures of new crystal forms containing the Escherichia coli enzyme and a comparative study of the known structures involving UDG.
Saikrishnan K, Bidya Sagar M, Ravishankar R, Roy S, Purnapatre K, Handa P, Varshney U, Vijayan M
Acta Crystallogr D Biol Crystallogr 58 1269-76 (2002)
PMID: 12136137

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 domains:

Structure analysis Details

Assemblies composition:
hetero dimer (preferred)
hetero tetramer
Assembly name:
PDBe Complex ID:
PDB-CPX-146129 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Uracil-DNA glycosylase Chains: A, B
Molecule details ›
Chains: A, B
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
Uracil-DNA glycosylase inhibitor Chains: C, D
Molecule details ›
Chains: C, D
Length: 84 amino acids
Theoretical weight: 9.48 KDa
Source organism: Bacillus phage PBS2
Expression system: Escherichia coli
UniProt:
  • Canonical: P14739 (Residues: 1-84; Coverage: 100%)
Gene name: UGI
Sequence domains: Uracil-DNA glycosylase inhibitor
Structure domains: Bacteriophage PBS2, uracil-glycosylase inhibitor

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU RU200
Spacegroup: P212121
Unit cell:
a: 51.164Å b: 89.902Å c: 141.776Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.183 0.183 0.277
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

4 mentions without citation

Exosites in the substrate specificity of blood coagulation reactions.
Bock et al. (2007)
3 more