Function and Biology Details
Reaction catalysed:
ADP-D-ribose + H(2)O = AMP + D-ribose 5-phosphate
Biochemical function:
Biological process:
Cellular component:
Sequence domains:
Structure domain:
Structure analysis Details
Assemblies composition:
Assembly name:
ADP-ribose pyrophosphatase (preferred)
PDBe Complex ID:
PDB-CPX-188086 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
ADP-ribose pyrophosphatase
Molecule details ›
Chains: A, B, C
Length: 220 amino acids
Theoretical weight: 24.88 KDa
Source organism: Escherichia coli
Expression system: Escherichia coli
UniProt:
Sequence domains: NUDIX domain
Structure domains: Nucleoside Triphosphate Pyrophosphohydrolase
Length: 220 amino acids
Theoretical weight: 24.88 KDa
Source organism: Escherichia coli
Expression system: Escherichia coli
UniProt:
- Canonical:
Q93K97 (Residues: 2-209; Coverage: 100%)
Sequence domains: NUDIX domain
Structure domains: Nucleoside Triphosphate Pyrophosphohydrolase
Ligands and Environments
No bound ligands
No modified residues
Experiments and Validation Details
X-ray source:
APS BEAMLINE 32-ID
Spacegroup:
P3221
Expression system: Escherichia coli
