› 1bsa

X-ray diffraction
2Å resolution

CRYSTAL STRUCTURAL ANALYSIS OF MUTATIONS IN THE HYDROPHOBIC CORES OF BARNASE

Released:
DOI: 10.2210/pdb1bsa/pdb
PDB entry 1bsa coloured by chain, front view.
PDB entry 1bsa coloured by chain, side view.
PDB entry 1bsa coloured by chain, top view.
Source organism: Bacillus amyloliquefaciens
Primary publication:
Crystal structural analysis of mutations in the hydrophobic cores of barnase.
Buckle AM, Henrick K, Fersht AR
J Mol Biol 234 847-60 (1993)
PMID: 8254677

Function and Biology Details

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-523745 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Ribonuclease Chains: A, B, C
Molecule details ›
Chains: A, B, C
Length: 110 amino acids
Theoretical weight: 12.38 KDa
Source organism: Bacillus amyloliquefaciens
Expression system: Not provided
UniProt:
  • Canonical: P00648 (Residues: 48-157; Coverage: 89%)
Sequence domains: ribonuclease
Structure domains: Microbial ribonucleases

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
Spacegroup: P32
Unit cell:
a: 58.63Å b: 58.63Å c: 81.87Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.173 not available not available
Expression system: Not provided

Quick links

Citations

4 review citations

Structure-function-rescue: the diverse nature of common p53 cancer mutants.
Joerger et al. (2007)
3 more

1 mention without citation

Interatomic potentials and solvation parameters from protein engineering data for buried residues.
Lomize et al. (2002)