› 5zde

X-ray diffraction
2.8Å resolution

Crystal structure of poly(ADP-ribose) glycohydrolase (PARG) from Deinococcus radiodurans in complex with ADP-ribose (P3221)

Released:
DOI: 10.2210/pdb5zde/pdb
PDB entry 5zde coloured by chain, front view.
PDB entry 5zde coloured by chain, side view.
PDB entry 5zde coloured by chain, top view.
Source organism: Deinococcus radiodurans R1
Primary publication:
Structural and biochemical evidence supporting poly ADP-ribosylation in the bacterium Deinococcus radiodurans.
Cho CC, Chien CY, Chiu YC, Lin MH, Hsu CH
OpenAccess logo Nat Commun 10 1491 (2019)
PMID: 30940816

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-577065 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Microbial-type PARG catalytic domain-containing protein Chain: C
Molecule details ›
Chain: C
Length: 251 amino acids
Theoretical weight: 27.39 KDa
Source organism: Deinococcus radiodurans R1
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: Q9RZM4 (Residues: 29-279; Coverage: 88%)
Gene name: DR_B0099
Sequence domains: Microbial-type PARG, catalytic domain

Ligands and Environments

1 bound ligand:
Ligand AR6 1 x AR6
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: NSRRC BEAMLINE BL13B1
Spacegroup: P3221
Unit cell:
a: 62.894Å b: 62.894Å c: 131.254Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.19 0.182 0.269
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

5 review citations

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

1 mention without citation

Structural and biochemical evidence supporting poly ADP-ribosylation in the bacterium Deinococcus radiodurans.
Cho et al. (2019)