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 P07268
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 (1)
| P07268 |
PRZN_SERME
Serratia sp. E-15
Serralysin
|
PDB Structure
| PDB | 1SRP |
| External Links | |
| Method | X-RAY DIFFRACTION |
| Organism | |
| Primary Citation |
Crystal structure of Serratia protease, a zinc-dependent proteinase from Serratia sp. E-15, containing a beta-sheet coil motif at 2.0 A resolution.
J.Biochem.(Tokyo)
|