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:
- Proteinase inhibitor I13, potato inhibitor I
- Peptidase S8, subtilisin-related
- Peptidase S8/S53 domain superfamily
- Proteinase inhibitor I13, potato inhibitor I superfamily
- Peptidase S8, subtilisin, Ser-active site
- Peptidase S8, subtilisin, His-active site
- Peptidase S8, subtilisin, Asp-active site
- Subtilisin Carlsberg-like catalytic domain
1 more domain
Structure domains:
Structure analysis Details
Assemblies composition:
Assembly name:
Subtilisin BPN' and Chymotrypsin inhibitor 2 (preferred)
PDBe Complex ID:
PDB-CPX-133535 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Subtilisin BPN'
Molecule details ›
Chain: E
Length: 281 amino acids
Theoretical weight: 28.38 KDa
Source organism: Bacillus amyloliquefaciens
Expression system: Bacillus subtilis
UniProt:
Sequence domains: Subtilase family
Structure domains: Peptidase S8/S53 domain
Length: 281 amino acids
Theoretical weight: 28.38 KDa
Source organism: Bacillus amyloliquefaciens
Expression system: Bacillus subtilis
UniProt:
- Canonical:
P00782 (Residues: 108-382; Coverage: 78%)
Sequence domains: Subtilase family
Structure domains: Peptidase S8/S53 domain
Chymotrypsin inhibitor 2
Molecule details ›
Chain: I
Length: 64 amino acids
Theoretical weight: 7.2 KDa
Source organism: Hordeum vulgare
Expression system: Escherichia coli BL21(DE3)
UniProt:
Sequence domains: Potato inhibitor I family
Structure domains: Trypsin Inhibitor V, subunit A
Length: 64 amino acids
Theoretical weight: 7.2 KDa
Source organism: Hordeum vulgare
Expression system: Escherichia coli BL21(DE3)
UniProt:
- Canonical: Q40059 (Residues: 21-84; Coverage: 76%)
Sequence domains: Potato inhibitor I family
Structure domains: Trypsin Inhibitor V, subunit A
