› 2g4k

X-ray diffraction
1.82Å 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:
Sequence domains:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-192676 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
ADP-ribosylhydrolase ARH3 Chain: A
Molecule details ›
Chain: A
Length: 347 amino acids
Theoretical weight: 37.84 KDa
Source organism: Homo sapiens
UniProt:
  • Canonical: Q9NX46 (Residues: 18-363; Coverage: 95%)
Gene names: ADPRHL2, ADPRS, ARH3
Sequence domains: ADP-ribosylglycohydrolase
Structure domains: ADP-ribosylation/Crystallin J1

Ligands and Environments

2 bound ligands:
Ligand MG 2 x MG
Ligand CL 2 x CL
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: EMBL/DESY, HAMBURG BEAMLINE X12
Spacegroup: P212121
Unit cell:
a: 57.03Å b: 59.34Å c: 98.71Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.192 0.191 0.247

Quick links

Citations

5 review citations

Conformational selection in trypsin-like proteases.
Pozzi et al. (2012)
4 more

1 mention without citation

Structure of mouse ADP-ribosylhydrolase 3 (mARH3).
Mueller-Dieckmann et al. (2008)