› 6hoz

X-ray diffraction
1.77Å resolution

ADP-ribosylserine hydrolase ARH3 of Latimeria chalumnae in complex with inosine diphosphate ribose (IDPr)

Released:
DOI: 10.2210/pdb6hoz/pdb
PDB entry 6hoz coloured by chain, front view.
PDB entry 6hoz coloured by chain, side view.
PDB entry 6hoz coloured by chain, top view.
Source organism: Latimeria chalumnae
Primary publication:
(ADP-ribosyl)hydrolases: Structural Basis for Differential Substrate Recognition and Inhibition.
Rack JGM, Ariza A, Drown BS, Henfrey C, Bartlett E, Shirai T, Hergenrother PJ, Ahel I
OpenAccess logo Cell Chem Biol 25 1533-1546.e12 (2018)
PMID: 30472116

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-124772 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
ADP-ribosylhydrolase ARH3 Chains: A, B
Molecule details ›
Chains: A, B
Length: 350 amino acids
Theoretical weight: 38.29 KDa
Source organism: Latimeria chalumnae
Expression system: Escherichia coli
UniProt:
  • Canonical: H3BCW1 (Residues: 10-356; Coverage: 98%)
Gene names: adprhl2, adprs, arh3
Sequence domains: ADP-ribosylglycohydrolase
Structure domains: ADP-ribosylation/Crystallin J1

Ligands and Environments

5 bound ligands:
Ligand MG 4 x MG
Ligand R5I 2 x R5I
Ligand R7I 2 x R7I
Ligand GOL 10 x GOL
Ligand ACT 1 x ACT
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: DIAMOND BEAMLINE I03
Spacegroup: P212121
Unit cell:
a: 66.844Å b: 96.933Å c: 107.519Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.16 0.158 0.189
Expression system: Escherichia coli

Quick links

Citations

13 review citations

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

1 mention without citation

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