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
Sequence domains:
Structure analysis Details
Assembly composition:
hetero dimer (preferred)
Assembly name:
Subtilisin BPN' (preferred)
PDBe Complex ID:
PDB-CPX-133531 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Subtilisin BPN'
Molecule details ›
Chain: P
Length: 80 amino acids
Theoretical weight: 8.79 KDa
Source organism: Bacillus amyloliquefaciens
Expression system: Escherichia coli
UniProt:
Sequence domains: Fervidolysin N-terminal prodomain
Structure domains: Peptidase S8 propeptide/proteinase inhibitor I9
Length: 80 amino acids
Theoretical weight: 8.79 KDa
Source organism: Bacillus amyloliquefaciens
Expression system: Escherichia coli
UniProt:
- Canonical:
P00782 (Residues: 32-107; Coverage: 21%)
Sequence domains: Fervidolysin N-terminal prodomain
Structure domains: Peptidase S8 propeptide/proteinase inhibitor I9
Subtilisin BPN'
Molecule details ›
Chain: S
Length: 266 amino acids
Theoretical weight: 26.42 KDa
Source organism: Bacillus amyloliquefaciens
Expression system: Escherichia coli
UniProt:
Sequence domains: Subtilase family
Structure domains: Peptidase S8/S53 domain
Length: 266 amino acids
Theoretical weight: 26.42 KDa
Source organism: Bacillus amyloliquefaciens
Expression system: Escherichia coli
UniProt:
- Canonical: P00782 (Residues: 108-382; Coverage: 76%)
Sequence domains: Subtilase family
Structure domains: Peptidase S8/S53 domain
