CATH Classification
| Level | CATH Code | Description |
|---|---|---|
|
3 | Alpha Beta |
|
3.40 | 3-Layer(aba) Sandwich |
|
3.40.390 | Collagenase (Catalytic Domain) |
|
3.40.390.10 | Collagenase (Catalytic Domain) |
Domain Context
CATH Clusters
| Superfamily | Collagenase (Catalytic Domain) |
| Functional Family | Serralysin |
Enzyme Information
| 3.4.24.40 |
Serralysin.
based on mapping to UniProt P23694
Preferential cleavage of bonds with hydrophobic residues in P1'.
-!- An extracellular endopeptidase from Pseudomonas aeruginosa, Escherichia freundii, Serratia marcescens and Erwinia chrysanthemi. -!- There is broad specificity in cleavage of the insulin B chain, with some species variations. -!- The pH optimum for digesting various proteins is about 9-10. -!- Belongs to peptidase family M10A. -!- Formerly EC 3.4.24.4.
|
UniProtKB Entries (2)
| P23694 |
PRZN_SERMA
Serratia marcescens
Serralysin
|
| P18958 |
INH_DICCH
Dickeya chrysanthemi
Proteinase inhibitor
|
PDB Structure
| PDB | 1SMP |
| External Links | |
| Method | X-RAY DIFFRACTION |
| Organism | Escherichia |
| Primary Citation |
Crystal structure of a complex between Serratia marcescens metallo-protease and an inhibitor from Erwinia chrysanthemi.
J.Mol.Biol.
|