3hfw

X-ray diffraction
1.92Å resolution

Crystal Structure of human ADP-ribosylhydrolase 1 (hARH1)

Released:
Source organism: Homo sapiens
Entry authors: Mueller-Dieckmann C, Weiss MS, Mueller-Dieckmann J, Koch-Nolte F

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:

Structure analysis Details

Assembly composition:
monomeric (preferred)
PDBe Complex ID:
PDB-CPX-157122 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
ADP-ribosylhydrolase ARH1 Chain: A
Molecule details ›
Chain: A
Length: 357 amino acids
Theoretical weight: 39.55 KDa
Source organism: Homo sapiens
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

No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE ID29
Spacegroup: P212121
Unit cell:
a: 45.28Å b: 52.79Å c: 140.34Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.156 0.155 0.185