› 6g2a

X-ray diffraction
1.8Å resolution

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

Released:
DOI: 10.2210/pdb6g2a/pdb
PDB entry 6g2a coloured by chain, front view.
PDB entry 6g2a coloured by chain, side view.
PDB entry 6g2a 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

4 bound ligands:
Ligand A3R 1 x A3R
Ligand MG 2 x MG
Ligand CL 1 x CL
Ligand ACT 3 x ACT
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: DIAMOND BEAMLINE I04
Spacegroup: C2
Unit cell:
a: 98.526Å b: 42.94Å c: 89.231Å
α: 90° β: 118.93° γ: 90°
R-values:
R R work R free
0.184 0.181 0.22
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)