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
- 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
- Peptidase S8/S53 domain
1 more domain
Structure domains:
Structure analysis Details
Assembly composition:
hetero dimer (preferred)
Assembly name:
Eglin C and Keratinase (preferred)
PDBe Complex ID:
PDB-CPX-109146 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Keratinase
Molecule details ›
Chain: E
Length: 274 amino acids
Theoretical weight: 27.31 KDa
Source organism: Bacillus subtilis
Expression system: Not provided
UniProt:
Structure domains: Peptidase S8/S53 domain
Length: 274 amino acids
Theoretical weight: 27.31 KDa
Source organism: Bacillus subtilis
Expression system: Not provided
UniProt:
- Canonical:
B0FXJ2 (Residues: 81-354; Coverage: 77%)
Structure domains: Peptidase S8/S53 domain
Eglin C
Molecule details ›
Chain: I
Length: 70 amino acids
Theoretical weight: 8.1 KDa
Source organism: Hirudo medicinalis
Expression system: Not provided
UniProt:
Structure domains: Trypsin Inhibitor V, subunit A
Length: 70 amino acids
Theoretical weight: 8.1 KDa
Source organism: Hirudo medicinalis
Expression system: Not provided
UniProt:
- Canonical: P01051 (Residues: 1-70; Coverage: 100%)
Structure domains: Trypsin Inhibitor V, subunit A
