Function and Biology Details
Reaction catalysed:
ADP-D-ribose + H(2)O = AMP + D-ribose 5-phosphate
Biochemical function:
Biological process:
- not assigned
Cellular component:
- not assigned
Structure analysis Details
Assembly composition:
homo dimer (preferred)
Assembly name:
Nudix hydrolase domain-containing protein (preferred)
PDBe Complex ID:
PDB-CPX-193255 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Nudix hydrolase domain-containing protein
Molecule details ›
Chains: A, B
Length: 145 amino acids
Theoretical weight: 15.61 KDa
Source organism: Deinococcus radiodurans R1
Expression system: Escherichia coli BL21(DE3)
UniProt:
Sequence domains: NUDIX domain
Structure domains: Nucleoside Triphosphate Pyrophosphohydrolase
Length: 145 amino acids
Theoretical weight: 15.61 KDa
Source organism: Deinococcus radiodurans R1
Expression system: Escherichia coli BL21(DE3)
UniProt:
- Canonical:
Q9RSC1 (Residues: 56-200; Coverage: 73%)
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:
ESRF BEAMLINE ID14-4
Spacegroup:
P43212
Expression system: Escherichia coli BL21(DE3)
