› 5lhb

X-ray diffraction
2.23Å resolution

Function and Biology Details

Reaction catalysed: 
Hydrolyzes poly(ADP-D-ribose) at glycosidic (1''-2') linkage of ribose-ribose bond to produce free ADP-D-ribose
Biochemical function:
Biological process:
Cellular component:
  • not assigned
Sequence domains:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-183229 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Poly(ADP-ribose) glycohydrolase Chain: A
Molecule details ›
Chain: A
Length: 531 amino acids
Theoretical weight: 61.1 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21
UniProt:
  • Canonical: Q86W56 (Residues: 448-976; Coverage: 54%)
Gene name: PARG
Sequence domains:

Ligands and Environments

3 bound ligands:
Ligand 6WJ 1 x 6WJ
Ligand SO4 3 x SO4
Ligand DMS 3 x DMS
1 modified residue:
Ligand 6WK 1 x 6WK

Experiments and Validation Details

Entry percentile scores
X-ray source: DIAMOND BEAMLINE I02
Spacegroup: P212121
Unit cell:
a: 67.01Å b: 89.73Å c: 95.44Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.165 0.162 0.212
Expression system: Escherichia coli BL21

Quick links

Citations

19 review citations

PARP and PARG inhibitors in cancer treatment.
Slade D. (2020)
18 more

1 mention without citation

β-Strand-mediated interactions of protein domains.
Bhat et al. (2020)