› 1ui1

X-ray diffraction
2.8Å resolution

Crystal Structure Of Uracil-DNA Glycosylase From Thermus Thermophilus HB8

Released:
DOI: 10.2210/pdb1ui1/pdb
PDB entry 1ui1 coloured by chain, front view.
PDB entry 1ui1 coloured by chain, side view.
PDB entry 1ui1 coloured by chain, top view.
Source organism: Thermus thermophilus
Primary publication:
Crystal structure of a family 4 uracil-DNA glycosylase from Thermus thermophilus HB8.
Hoseki J, Okamoto A, Masui R, Shibata T, Inoue Y, Yokoyama S, Kuramitsu S
J Mol Biol 333 515-26 (2003)
PMID: 14556741

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-178079 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Type-4 uracil-DNA glycosylase Chain: A
Molecule details ›
Chain: A
Length: 205 amino acids
Theoretical weight: 23.19 KDa
Source organism: Thermus thermophilus
Expression system: Escherichia coli
UniProt:
  • Canonical: Q5SKC5 (Residues: 1-205; Coverage: 100%)
Gene names: TTHA0718, udg
Sequence domains: Uracil DNA glycosylase superfamily
Structure domains: Uracil-DNA glycosylase-like domain

Ligands and Environments

1 bound ligand:
Ligand SF4 1 x SF4
1 modified residue:
Ligand MSE 4 x MSE

Experiments and Validation Details

Entry percentile scores
X-ray source: SPRING-8 BEAMLINE BL45XU
Spacegroup: P212121
Unit cell:
a: 45.502Å b: 59.034Å c: 81.404Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.214 0.214 0.276
Expression system: Escherichia coli

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Citations

6 review citations

DNA base damage recognition and removal: new twists and grooves.
Huffman et al. (2005)
5 more

2 mentions without citation

Targeting severe acute respiratory syndrome-coronavirus (SARS-CoV-1) with structurally diverse inhibitors: a comprehensive review.
Hosseini-Zare et al. (2020)
1 more