CATH Classification
| Level | CATH Code | Description |
|---|---|---|
|
2 | Mainly Beta |
|
2.60 | Sandwich |
|
2.60.120 | Jelly Rolls |
|
2.60.120.380 |
Domain Context
CATH Clusters
| Superfamily | 2.60.120.380 |
| Functional Family | Subtilisin-like serine protease |
Enzyme Information
| 3.4.21.62 |
Subtilisin.
based on mapping to UniProt Q5JIZ5
Hydrolysis of proteins with broad specificity for peptide bonds, and a preference for a large uncharged residue in P1. Hydrolyzes peptide amides.
-!- Subtilisin is a serine endopeptidase that evolved independently of chymotrypsin. -!- It contains no cysteine residues (although these are found in homologous enzymes). -!- Species variants include subtilisin BPN' (also subtilisin B, subtilopeptidase C, nagarse, nagarse proteinase, subtilisin Novo, bacterial proteinase Novo) and subtilisin Carlsberg (subtilisin A, subtilopeptidase A, alcalase Novo). -!- Similar enzymes are produced by various Bacillus subtilis strains and other Bacillus species. -!- Belongs to peptidase family S8. -!- Formerly EC 3.4.4.16 and EC 3.4.21.14.
|
UniProtKB Entries (1)
| Q5JIZ5 |
TKSP_THEKO
Thermococcus kodakarensis KOD1
Subtilisin-like serine protease
|
PDB Structure
| PDB | 3AFG |
| External Links | |
| Method | X-RAY DIFFRACTION |
| Organism | |
| Primary Citation |
Crystal structure of a subtilisin homologue, Tk-SP, from Thermococcus kodakaraensis: requirement of a C-terminal beta-jelly roll domain for hyperstability.
J.Mol.Biol.
|
