› 5zqy

X-ray diffraction
1.58Å resolution

Crystal structure of a poly(ADP-ribose) glycohydrolase

Released:
DOI: 10.2210/pdb5zqy/pdb
PDB entry 5zqy coloured by chain, front view.
PDB entry 5zqy coloured by chain, side view.
PDB entry 5zqy coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Structure-function analyses reveal the mechanism of the ARH3-dependent hydrolysis of ADP-ribosylation.
Wang M, Yuan Z, Xie R, Ma Y, Liu X, Yu X
J Biol Chem 293 14470-14480 (2018)
PMID: 30045870

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: 349 amino acids
Theoretical weight: 37.85 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

2 bound ligands:
Ligand MG 2 x MG
Ligand AR6 1 x AR6
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SSRF BEAMLINE BL17U1
Spacegroup: P21
Unit cell:
a: 43.88Å b: 76.74Å c: 48.53Å
α: 90° β: 103° γ: 90°
R-values:
R R work R free
0.158 0.157 0.18
Expression system: Escherichia coli

Quick links

Citations

7 review citations

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

4 mentions without citation

(ADP-ribosyl)hydrolases: Structural Basis for Differential Substrate Recognition and Inhibition.
Rack et al. (2018)
3 more