6iux

X-ray diffraction
1.2Å resolution

Crystal structure of a hydrolase protein

Released:
Source organism: Homo sapiens
Entry authors: Liu XH, Yu XC

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: 379 amino acids
Theoretical weight: 41.97 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: P54922 (Residues: 2-357; Coverage: 100%)
Gene names: ADPRH, ARH1
Sequence domains: ADP-ribosylglycohydrolase

Ligands and Environments

2 bound ligands:
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SSRF BEAMLINE BL17U
Spacegroup: P212121
Unit cell:
a: 45.68Å b: 52.919Å c: 141.24Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.16 0.159 0.183
Expression system: Escherichia coli