› 2foz

X-ray diffraction
1.6Å resolution

human ADP-ribosylhydrolase 3

Released:
DOI: 10.2210/pdb2foz/pdb
PDB entry 2foz coloured by chain, front view.
PDB entry 2foz coloured by chain, side view.
PDB entry 2foz coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
The structure of human ADP-ribosylhydrolase 3 (ARH3) provides insights into the reversibility of protein ADP-ribosylation.
Mueller-Dieckmann C, Kernstock S, Lisurek M, von Kries JP, Haag F, Weiss MS, Koch-Nolte F
Proc Natl Acad Sci U S A 103 15026-31 (2006)
PMID: 17015823

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: 37.76 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: Q9NX46 (Residues: 19-363; Coverage: 95%)
Gene names: ADPRHL2, ADPRS, ARH3
Sequence domains: ADP-ribosylglycohydrolase
Structure domains: ADP-ribosylation/Crystallin J1

Ligands and Environments

1 bound ligand:
Ligand MG 2 x MG
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: EMBL/DESY, HAMBURG BEAMLINE BW7A
Spacegroup: P212121
Unit cell:
a: 56.3Å b: 60.4Å c: 97.2Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.175 0.175 0.209
Expression system: Escherichia coli

Quick links

Citations

36 review citations

The multifaceted roles of PARP1 in DNA repair and chromatin remodelling.
Ray Chaudhuri et al. (2017)
35 more

14 mentions without citation

(ADP-ribosyl)hydrolases: structure, function, and biology.
Rack et al. (2020)
13 more