PDBe 1st2

X-ray diffraction
2Å resolution

THE THREE-DIMENSIONAL STRUCTURE OF BACILLUS AMYLOLIQUEFACIENS SUBTILISIN AT 1.8 ANGSTROMS AND AN ANALYSIS OF THE STRUCTURAL CONSEQUENCES OF PEROXIDE INACTIVATION

Released:

Function and Biology Details

Reaction catalysed:
Hydrolysis of proteins with broad specificity for peptide bonds, and a preference for a large uncharged residue in P1. Hydrolyzes peptide amides.
Biochemical function:
Biological process:
Cellular component:
  • not assigned

Structure analysis Details

Assembly composition:
monomeric (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Subtilisin BPN' Chain: A
Molecule details ›
Chain: A
Length: 275 amino acids
Theoretical weight: 27.6 KDa
Source organism: Bacillus amyloliquefaciens
Expression system: Escherichia coli
UniProt:
  • Canonical: P00782 (Residues: 108-382; Coverage: 78%)
Gene name: apr
Sequence domains: Subtilase family
Structure domains: Peptidase S8/S53 domain

Ligands and Environments

2 bound ligands:

1 modified residue:

Experiments and Validation Details

Entry percentile scores
Spacegroup: P212121
Unit cell:
a: 39.3Å b: 72.8Å c: 75.35Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.168 0.168 not available
Expression system: Escherichia coli