› 6d3a

X-ray diffraction
1.6Å resolution

Structure of human ARH3 D314E bound to ADP-ribose and magnesium

Released:
DOI: 10.2210/pdb6d3a/pdb
PDB entry 6d3a coloured by chain, front view.
PDB entry 6d3a coloured by chain, side view.
PDB entry 6d3a coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Structure of human ADP-ribosyl-acceptor hydrolase 3 bound to ADP-ribose reveals a conformational switch that enables specific substrate recognition.
Pourfarjam Y, Ventura J, Kurinov I, Cho A, Moss J, Kim IK
J Biol Chem 293 12350-12359 (2018)
PMID: 29907568

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 Chains: A, B, C, D
Molecule details ›
Chains: A, B, C, D
Length: 366 amino acids
Theoretical weight: 39.29 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: Q9NX46 (Residues: 1-363; Coverage: 100%)
Gene names: ADPRHL2, ADPRS, ARH3
Sequence domains: ADP-ribosylglycohydrolase
Structure domains: ADP-ribosylation/Crystallin J1

Ligands and Environments

2 bound ligands:
Ligand AR6 4 x AR6
Ligand MG 4 x MG
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 24-ID-E
Spacegroup: P1
Unit cell:
a: 44.901Å b: 72.229Å c: 115.906Å
α: 83.008° β: 85.733° γ: 72.43°
R-values:
R R work R free
0.169 0.167 0.198
Expression system: Escherichia coli

Quick links

Citations

10 review citations

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

1 mention without citation

Structure of human ADP-ribosyl-acceptor hydrolase 3 bound to ADP-ribose reveals a conformational switch that enables specific substrate recognition.
Pourfarjam et al. (2018)