› 3a6t

X-ray diffraction
1.96Å resolution

Function and Biology Details

Reaction catalysed: 
8-oxo-dGTP + H(2)O = 8-oxo-dGMP + diphosphate
Biochemical function:
Biological process:
Cellular component:
  • not assigned
Sequence domains:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-140099 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecules (2 distinct):
8-oxo-dGTP diphosphatase Chain: A
Molecule details ›
Chain: A
Length: 129 amino acids
Theoretical weight: 14.95 KDa
Source organism: Escherichia coli K-12
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: P08337 (Residues: 1-129; Coverage: 100%)
Gene names: JW0097, b0099, mutT
Sequence domains: NUDIX domain
Structure domains: Nucleoside Triphosphate Pyrophosphohydrolase

Ligands and Environments

Carbohydrate polymer : NEW Components: GLC, FRU
Carbohydrate polymer
3 bound ligands:
Ligand NA 1 x NA
Ligand SO4 2 x SO4
Ligand 8OG 1 x 8OG
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SPRING-8 BEAMLINE BL41XU, SPRING-8 BEAMLINE BL38B1
Spacegroup: P212121
Unit cell:
a: 37.972Å b: 56.007Å c: 59.369Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.178 0.178 0.201
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

2 review citations

The BER necessities: the repair of DNA damage in human-adapted bacterial pathogens.
van der Veen et al. (2015)
1 more

8 mentions without citation

Noncatalytic Domains in DNA Glycosylases.
Torgasheva et al. (2022)
7 more