› 1sno

X-ray diffraction
1.7Å resolution

PROTEIN STABILITY IN STAPHYLOCOCCAL NUCLEASE

Released:
DOI: 10.2210/pdb1sno/pdb
PDB entry 1sno coloured by chain, front view.
PDB entry 1sno coloured by chain, side view.
PDB entry 1sno coloured by chain, top view.
Source organism: Staphylococcus aureus
Primary publication:
Coupling between trans/cis proline isomerization and protein stability in staphylococcal nuclease.
Truckses DM, Somoza JR, Prehoda KE, Miller SC, Markley JL
Protein Sci 5 1907-16 (1996)
PMID: 8880915

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
Sequence domains:
Structure domain:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-523735 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Nuclease A Chain: A
Molecule details ›
Chain: A
Length: 149 amino acids
Theoretical weight: 16.82 KDa
Source organism: Staphylococcus aureus
Expression system: Escherichia coli
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: 47.74Å b: 47.74Å c: 63.71Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.17 0.17 0.224
Expression system: Escherichia coli

Quick links

Citations

1 review citation

Cis-trans isomerization of omega dihedrals in proteins.
Craveur et al. (2013)
21 other articles

14 mentions without citation

A Halogen Bonding Perspective on Iodothyronine Deiodinase Activity.
Marsan et al. (2020)
13 more