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
- Hemolysin-type calcium-binding conserved site
- RTX calcium-binding nonapeptide repeat
- Peptidase M10 serralysin, C-terminal
- Peptidase, metallopeptidase
- Serralysin-like metallopeptidase domain
- Metallopeptidase, catalytic domain superfamily
3 more domains
Structure analysis Details
Assembly composition:
hetero dimer (preferred)
Assembly name:
Serralysin and Proteinase inhibitor (preferred)
PDBe Complex ID:
PDB-CPX-169816 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Serralysin
Molecule details ›
Chain: P
Length: 470 amino acids
Theoretical weight: 49.53 KDa
Source organism: Pseudomonas aeruginosa
Expression system: Escherichia coli BL21(DE3)
UniProt:
Sequence domains:
Length: 470 amino acids
Theoretical weight: 49.53 KDa
Source organism: Pseudomonas aeruginosa
Expression system: Escherichia coli BL21(DE3)
UniProt:
- Canonical:
Q03023 (Residues: 10-479; Coverage: 98%)
Sequence domains:
- Metallo-peptidase family M12B Reprolysin-like
- Peptidase M10 serralysin C terminal
- RTX calcium-binding nonapeptide repeat (4 copies)
Proteinase inhibitor
Molecule details ›
Chain: I
Length: 106 amino acids
Theoretical weight: 11.4 KDa
Source organism: Pseudomonas aeruginosa
Expression system: Escherichia coli BL21(DE3)
UniProt:
Sequence domains: Protease inhibitor Inh
Structure domains: Lipocalin
Length: 106 amino acids
Theoretical weight: 11.4 KDa
Source organism: Pseudomonas aeruginosa
Expression system: Escherichia coli BL21(DE3)
UniProt:
- Canonical: Q03026 (Residues: 26-131; Coverage: 100%)
Sequence domains: Protease inhibitor Inh
Structure domains: Lipocalin
