› 6g28

X-ray diffraction
1.23Å resolution

Human [protein ADP-ribosylargenine] hydrolase ARH1 in complex with ADP-ribose

Released:
DOI: 10.2210/pdb6g28/pdb
PDB entry 6g28 coloured by chain, front view.
PDB entry 6g28 coloured by chain, side view.
PDB entry 6g28 coloured by chain, top view.
Source organism: Homo sapiens
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
Cell Chem Biol 25 1533-1546.e12 (2018)
PMID: 30472116

Function and Biology Details

Reaction catalysed: 
N(omega)-(ADP-D-ribosyl)-L-arginine + H(2)O = ADP-D-ribose + L-arginine
Biochemical function:
Biological process:
Cellular component:
Sequence domains:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-157122 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
ADP-ribosylhydrolase ARH1 Chain: A
Molecule details ›
Chain: A
Length: 367 amino acids
Theoretical weight: 40.68 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: P54922 (Residues: 1-357; Coverage: 100%)
Gene names: ADPRH, ARH1
Sequence domains: ADP-ribosylglycohydrolase
Structure domains: ADP-ribosylation/Crystallin J1

Ligands and Environments

3 bound ligands:
Ligand AR6 1 x AR6
Ligand MG 2 x MG
Ligand CL 3 x CL
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: DIAMOND BEAMLINE I03
Spacegroup: P212121
Unit cell:
a: 64.102Å b: 66.687Å c: 83.42Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.146 0.145 0.157
Expression system: Escherichia coli

Quick links

Citations

11 review citations

Cellular stress leads to the formation of membraneless stress assemblies in eukaryotic cells.
van Leeuwen et al. (2019)
10 more

4 mentions without citation

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