PDBe 2sns

X-ray diffraction
1.5Å resolution

STAPHYLOCOCCAL NUCLEASE. PROPOSED MECHANISM OF ACTION BASED ON STRUCTURE OF ENZYME-THYMIDINE 3(PRIME),5(PRIME)-BIPHOSPHATE-CALCIUM ION COMPLEX AT 1.5-ANGSTROMS RESOLUTION

Released:
Source organism: Staphylococcus aureus
Primary publication:
Thesis, Texas Agricultural and Mechanical University (1977)

Function and Biology Details

Reaction catalysed:
Endonucleolytic cleavage to nucleoside 3'-phosphates and 3'-phosphooligonucleotide end-products. 
Biochemical function:
  • not assigned
Biological process:
  • not assigned
Cellular component:
  • not assigned

Structure analysis Details

Assembly composition:
monomeric (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Nuclease A Chain: A
Molecule details ›
Chain: A
Length: 149 amino acids
Theoretical weight: 16.84 KDa
Source organism: Staphylococcus aureus
Expression system: Not provided
UniProt:
  • Canonical: P00644 (Residues: 83-231; Coverage: 73%)
Gene name: nuc
Sequence domains: Staphylococcal nuclease homologue
Structure domains: OB fold (Dihydrolipoamide Acetyltransferase, E2P)

Ligands and Environments

2 bound ligands:

No modified residues

Experiments and Validation Details

Entry percentile scores
Spacegroup: P41
Unit cell:
a: 48.19Å b: 48.19Å c: 63.4Å
α: 90° β: 90° γ: 90°
Expression system: Not provided