PDBe 1sca

X-ray diffraction
2Å resolution

ENZYME CRYSTAL STRUCTURE IN A NEAT ORGANIC SOLVENT

Released:
Source organism: Bacillus licheniformis
Primary publication:
Enzyme crystal structure in a neat organic solvent.
Proc. Natl. Acad. Sci. U.S.A. 90 8653-7 (1993)
PMID: 8378343

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 Carlsberg Chain: A
Molecule details ›
Chain: A
Length: 274 amino acids
Theoretical weight: 27.31 KDa
Source organism: Bacillus licheniformis
Expression system: Not provided
UniProt:
  • Canonical: P00780 (Residues: 106-379; Coverage: 78%)
Gene name: apr
Sequence domains: Subtilase family
Structure domains: Rossmann fold

Ligands and Environments

2 bound ligands:

No modified residues

Experiments and Validation Details

Entry percentile scores
Spacegroup: P212121
Unit cell:
a: 76.5Å b: 55.3Å c: 53.4Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.156 not available not available
Expression system: Not provided