› 1snm

X-ray diffraction
1.74Å resolution

ACTIVE SITE MUTANT GLU-43 (RIGHT ARROW) ASP IN STAPHYLOCOCCAL NUCLEASE DISPLAYS NONLOCAL STRUCTURAL CHANGES

Released:
DOI: 10.2210/pdb1snm/pdb
PDB entry 1snm coloured by chain, front view.
PDB entry 1snm coloured by chain, side view.
PDB entry 1snm coloured by chain, top view.
Source organism: Staphylococcus aureus
Primary publication:
Active site mutant Glu-43----Asp in staphylococcal nuclease displays nonlocal structural changes.
Loll PJ, Lattman EE
Biochemistry 29 6866-73 (1990)
PMID: 2397218

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: 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

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: 48.59Å b: 48.59Å c: 63.38Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.174 not available not available
Expression system: Not provided

Quick links

Citations

3 review citations

Quantitative interpretations of double mutations of enzymes.
Mildvan et al. (1992)
2 more

1 mention without citation

Chemical shift prediction for protein structure calculation and quality assessment using an optimally parameterized force field.
Nielsen et al. (2012)