› 1eya

X-ray diffraction
2Å resolution

STRUCTURE OF S. NUCLEASE STABILIZING QUINTUPLE MUTANT T33V/T41I/P117G/H124L/S128A

Released:
DOI: 10.2210/pdb1eya/pdb
PDB entry 1eya coloured by chain, front view.
PDB entry 1eya coloured by chain, side view.
PDB entry 1eya coloured by chain, top view.
Source organism: Staphylococcus aureus
Primary publication:
Increasing the thermostability of staphylococcal nuclease: implications for the origin of protein thermostability.
Chen J, Lu Z, Sakon J, Stites WE
J Mol Biol 303 125-30 (2000)
PMID: 11023780

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: 16.77 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
X-ray source: RIGAKU RUH3R
Spacegroup: P41
Unit cell:
a: 49.181Å b: 49.181Å c: 63.734Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.181 not available 0.288
Expression system: Escherichia coli

Quick links

Citations

4 review citations

Energetics of protein folding.
Baldwin RL. (2007)
3 more

2 mentions without citation

Hysteretic and graded responses in bacterial two-component signal transduction.
Igoshin et al. (2008)
1 more