Function and Biology Details
Reaction catalysed:
Endonucleolytic cleavage to nucleoside 3'-phosphates and 3'-phosphooligonucleotide end-products
Biochemical function:
Biological process:
- not assigned
Cellular component:
- not assigned
Structure analysis Details
Assembly composition:
monomeric (preferred)
Assembly name:
Thermonuclease (preferred)
PDBe Complex ID:
PDB-CPX-107535 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Thermonuclease
Molecule details ›
Chain: A
Length: 140 amino acids
Theoretical weight: 15.91 KDa
Source organism: Staphylococcus aureus
Expression system: Escherichia coli
UniProt:
Sequence domains: Staphylococcal nuclease homologue
Structure domains: OB fold (Dihydrolipoamide Acetyltransferase, E2P)
Length: 140 amino acids
Theoretical weight: 15.91 KDa
Source organism: Staphylococcus aureus
Expression system: Escherichia coli
UniProt:
- Canonical:
A5A523 (Residues: 69-208; Coverage: 84%)
Sequence domains: Staphylococcal nuclease homologue
Structure domains: OB fold (Dihydrolipoamide Acetyltransferase, E2P)
Ligands and Environments
No bound ligands
No modified residues
Experiments and Validation Details
Chemical shift assignment:
88%
Refinement method:
molecular dynamics, simulated annealing
Expression system: Escherichia coli
