1kda

X-ray diffraction
1.9Å resolution

STABILIZATION OF A STRAINED PROTEIN LOOP CONFORMATION THROUGH PROTEIN ENGINEERING

Released:
Source organism: Staphylococcus aureus

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:
PDBe Complex ID:
PDB-CPX-132790 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Nuclease A Chain: A
Molecule details ›
Chain: A
Length: 149 amino acids
Theoretical weight: 16.83 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

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
Spacegroup: P41
Unit cell:
a: 48.2Å b: 48.2Å c: 63.1Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.189 0.189 not available
Expression system: Not provided