› 5m31

X-ray diffraction
1.67Å resolution

Macrodomain of Thermus aquaticus DarG

Released:
DOI: 10.2210/pdb5m31/pdb
PDB entry 5m31 coloured by chain, front view.
PDB entry 5m31 coloured by chain, side view.
PDB entry 5m31 coloured by chain, top view.
Source organism: Thermus aquaticus Y51MC23
Primary publication:
The Toxin-Antitoxin System DarTG Catalyzes Reversible ADP-Ribosylation of DNA.
Jankevicius G, Ariza A, Ahel M, Ahel I
Mol Cell 64 1109-1116 (2016)
PMID: 27939941

Function and Biology Details

Biochemical function:
  • not assigned
Biological process:
  • not assigned
Cellular component:
  • not assigned
Sequence domains:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-145140 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
DNA ADP-ribosyl glycohydrolase Chain: A
Molecule details ›
Chain: A
Length: 165 amino acids
Theoretical weight: 18.78 KDa
Source organism: Thermus aquaticus Y51MC23
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: P0DV57 (Residues: 1-155; Coverage: 43%)
Gene names: TO73_1569, darG
Sequence domains: Macro domain

Ligands and Environments

2 bound ligands:
Ligand GOL 2 x GOL
Ligand CL 3 x CL
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: DIAMOND BEAMLINE I02
Spacegroup: C2
Unit cell:
a: 103.6Å b: 45.02Å c: 35.54Å
α: 90° β: 101.25° γ: 90°
R-values:
R R work R free
0.173 0.172 0.203
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

37 review citations

PARPs and ADP-ribosylation: recent advances linking molecular functions to biological outcomes.
Gupte et al. (2017)
36 more

1 mention without citation

ADP-ribosylation systems in bacteria and viruses.
Mikolčević et al. (2021)