› 7kg0

X-ray diffraction
1.66Å 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: 61.02 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: Q86W56 (Residues: 448-976; Coverage: 54%)
Gene name: PARG
Sequence domains:

Ligands and Environments

3 bound ligands:
Ligand WDA 1 x WDA
Ligand EDO 1 x EDO
Ligand SO4 4 x SO4
1 modified residue:
Ligand CME 1 x CME

Experiments and Validation Details

Entry percentile scores
X-ray source: SSRL BEAMLINE BL12-2
Spacegroup: P21
Unit cell:
a: 45.293Å b: 66.579Å c: 89.142Å
α: 90° β: 95.5° γ: 90°
R-values:
R R work R free
0.186 0.185 0.219
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

12 review citations

Structural biology of SARS-CoV-2: open the door for novel therapies.
Yan et al. (2022)
11 more

1 mention without citation

Targeting SARS-CoV-2 Nsp3 macrodomain structure with insights from human poly(ADP-ribose) glycohydrolase (PARG) structures with inhibitors.
Brosey et al. (2021)