3sig

X-ray diffraction
1.28Å resolution

The X-ray crystal structure of poly(ADP-ribose) glycohydrolase (PARG) bound to ADP-ribose from Thermomonospora curvata

Released:

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:
  • not assigned
Biological process:
  • not assigned
Cellular component:
  • not assigned

Structure analysis Details

Assembly composition:
monomeric (preferred)
PDBe Complex ID:
PDB-CPX-112243 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Microbial-type PARG catalytic domain-containing protein Chain: A
Molecule details ›
Chain: A
Length: 277 amino acids
Theoretical weight: 29.76 KDa
Source organism: Thermomonospora curvata DSM 43183
Expression system: Escherichia coli
UniProt:
  • Canonical: D1AC29 (Residues: 40-316; Coverage: 88%)
Gene name: Tcur_1721
Sequence domains: Microbial-type PARG, catalytic domain
Structure domains: Leucine Aminopeptidase, subunit E, domain 1

Ligands and Environments

1 bound ligand:
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: DIAMOND BEAMLINE I04
Spacegroup: P212121
Unit cell:
a: 50.13Å b: 106.39Å c: 44.16Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.15 0.149 0.161
Expression system: Escherichia coli