› 1stb

X-ray diffraction
2Å resolution

ACCOMMODATION OF INSERTION MUTATIONS ON THE SURFACE AND IN THE INTERIOR OF STAPHYLOCOCCAL NUCLEASE

Released:
DOI: 10.2210/pdb1stb/pdb
PDB entry 1stb coloured by chain, front view.
PDB entry 1stb coloured by chain, side view.
PDB entry 1stb coloured by chain, top view.
Source organism: Staphylococcus aureus
Primary publication:
Accommodation of insertion mutations on the surface and in the interior of staphylococcal nuclease.
Keefe LJ, Quirk S, Gittis A, Sondek J, Lattman EE
Protein Sci 3 391-401 (1994)
PMID: 8019410

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-132790 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Nuclease A Chain: A
Molecule details ›
Chain: A
Length: 150 amino acids
Theoretical weight: 16.96 KDa
Source organism: Staphylococcus aureus
Expression system: Not provided
UniProt:
  • Canonical: P00644 (Residues: 83-117, 119-120, 121-231; Coverage: 72%)
Gene name: nuc
Sequence domains: Staphylococcal nuclease homologue
Structure domains: OB fold (Dihydrolipoamide Acetyltransferase, E2P)

Ligands and Environments

2 bound ligands:
Ligand CA 1 x CA
Ligand THP 1 x THP
No modified residues

Experiments and Validation Details

Entry percentile scores
Spacegroup: P41
Unit cell:
a: 47.16Å b: 47.16Å c: 63.15Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.196 0.196 not available
Expression system: Not provided

Quick links

Citations

1 review citation

The emerging role of insertions and deletions in protein engineering.
Shortle et al. (1995)
12 other articles