› 1jor

Solution NMR

Ensemble structures for unligated Staphylococcal nuclease-H124L

Released:
DOI: 10.2210/pdb1jor/pdb
PDB entry 1jor coloured by chain, ensemble of 30 models, front view.
PDB entry 1jor coloured by chain, ensemble of 30 models, side view.
PDB entry 1jor coloured by chain, ensemble of 30 models, top view.
Source organism: Staphylococcus aureus
Primary publication:
Solution structures of staphylococcal nuclease from multidimensional, multinuclear NMR: nuclease-H124L and its ternary complex with Ca2+ and thymidine-3',5'-bisphosphate.
Wang J, Truckses DM, Abildgaard F, Dzakula Z, Zolnai Z, Markley JL
J Biomol NMR 10 143-64 (1997)
PMID: 9369015

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 BL21(DE3)
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
Refinement method: Distance, hydrogen bond and torsion angle constraints
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

1 review citation

Lessons from pressure denaturation of proteins.
Roche et al. (2018)
22 other articles

7 mentions without citation

The implementation of SOMO (SOlution MOdeller) in the UltraScan analytical ultracentrifugation data analysis suite: enhanced capabilities allow the reliable hydrodynamic modeling of virtually any kind of biomacromolecule.
Brookes et al. (2010)
6 more