Function and Biology Details
Reaction catalysed:
Cyclic di-3',5'-adenylate + H(2)O = 5'-O-phosphonoadenylyl-(3'->5')-adenosine
Biochemical function:
- not assigned
Biological process:
- not assigned
Cellular component:
- not assigned
Structure analysis Details
Assembly composition:
homo dimer (preferred)
Assembly name:
Cyclic-di-AMP phosphodiesterase GdpP (preferred)
PDBe Complex ID:
PDB-CPX-107352 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Cyclic-di-AMP phosphodiesterase GdpP
Molecule details ›
Chains: A, B
Length: 113 amino acids
Theoretical weight: 13.21 KDa
Source organism: Geobacillus thermodenitrificans NG80-2
Expression system: Escherichia coli BL21(DE3)
UniProt:
Sequence domains: Cyclic-di-AMP phosphodiesterase GdpP, PAS domain
Structure domains: PAS domain
Length: 113 amino acids
Theoretical weight: 13.21 KDa
Source organism: Geobacillus thermodenitrificans NG80-2
Expression system: Escherichia coli BL21(DE3)
UniProt:
- Canonical:
A4ITV2 (Residues: 55-162; Coverage: 16%)
Sequence domains: Cyclic-di-AMP phosphodiesterase GdpP, PAS domain
Structure domains: PAS domain
Ligands and Environments
No bound ligands
No modified residues
Experiments and Validation Details
Chemical shift assignment:
45%
Expression system: Escherichia coli BL21(DE3)
