› 7l9i

X-ray diffraction
1.8Å resolution

Crystal structure of human ARH3-D314A bound to magnesium and ADP-ribose

Released:
DOI: 10.2210/pdb7l9i/pdb
PDB entry 7l9i coloured by chain, front view.
PDB entry 7l9i coloured by chain, side view.
PDB entry 7l9i coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Structural and biochemical analysis of human ADP-ribosyl-acceptor hydrolase 3 reveals the basis of metal selectivity and different roles for the two magnesium ions.
Pourfarjam Y, Ma Z, Kurinov I, Moss J, Kim IK
J Biol Chem 296 100692
PMID: 33894202

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: 39.23 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

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: 44.808Å b: 71.428Å c: 115.803Å
α: 94.033° β: 94.626° γ: 107.86°
R-values:
R R work R free
0.191 0.189 0.228
Expression system: Escherichia coli

Quick links

Citations

1 review citation

ARH Family of ADP-Ribose-Acceptor Hydrolases.
Ishiwata-Endo et al. (2022)

1 mention without citation

Structural and biochemical analysis of human ADP-ribosyl-acceptor hydrolase 3 reveals the basis of metal selectivity and different roles for the two magnesium ions.
Pourfarjam et al. (2021)