Function and Biology Details
Reaction catalysed:
Preferential cleavage of bonds with hydrophobic residues in P1'.
Biochemical function:
Biological process:
Cellular component:
Sequence domains:
- Protease inhibitor
- Serralysin-like metalloprotease, C-terminal
- Alkaline proteinase inhibitor/ Outer membrane lipoprotein Omp19
- Protease inhibitor, beta-barrel domain
- Hemolysin-type calcium-binding conserved site
- RTX calcium-binding nonapeptide repeat
- Peptidase M10 serralysin, C-terminal
- Peptidase M10, metallopeptidase
4 more domains
Structure analysis Details
Assembly composition:
hetero dimer (preferred)
Assembly name:
Proteinase inhibitor and Serralysin (preferred)
PDBe Complex ID:
PDB-CPX-148482 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Serralysin
Molecule details ›
Chain: A
Length: 471 amino acids
Theoretical weight: 50.44 KDa
Source organism: Serratia marcescens
Expression system: Escherichia coli
UniProt:
Structure domains:
Length: 471 amino acids
Theoretical weight: 50.44 KDa
Source organism: Serratia marcescens
Expression system: Escherichia coli
UniProt:
- Canonical:
P23694 (Residues: 17-487; Coverage: 97%)
Structure domains:
Proteinase inhibitor
Molecule details ›
Chain: I
Length: 101 amino acids
Theoretical weight: 11.02 KDa
Source organism: Dickeya chrysanthemi
Expression system: Escherichia coli
UniProt:
Sequence domains: Protease inhibitor Inh
Structure domains: Lipocalin
Length: 101 amino acids
Theoretical weight: 11.02 KDa
Source organism: Dickeya chrysanthemi
Expression system: Escherichia coli
UniProt:
- Canonical: P18958 (Residues: 20-120; Coverage: 100%)
Sequence domains: Protease inhibitor Inh
Structure domains: Lipocalin
