CATH Classification
| Level | CATH Code | Description |
|---|---|---|
|
3 | Alpha Beta |
|
3.40 | 3-Layer(aba) Sandwich |
|
3.40.50 | Rossmann fold |
|
3.40.50.200 | Peptidase S8/S53 domain |
Domain Context
CATH Clusters
| Superfamily | Peptidase S8/S53 domain |
| Functional Family |
Enzyme Information
| 3.4.21.62 |
Subtilisin.
based on mapping to UniProt P00780
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 (2)
| P00780 |
SUBT_BACLI
Bacillus licheniformis
Subtilisin Carlsberg
|
| P01051 |
ICIC_HIRME
Hirudo medicinalis
Eglin C
|
PDB Structure
| PDB | 2SEC |
| External Links | |
| Method | X-RAY DIFFRACTION |
| Organism | |
| Primary Citation |
Structural comparison of two serine proteinase-protein inhibitor complexes: eglin-c-subtilisin Carlsberg and CI-2-subtilisin Novo.
Biochemistry
|