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 | Tk-subtilisin |
Enzyme Information
| 3.4.21.62 |
Subtilisin.
based on mapping to UniProt P00782
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)
| P01051 |
ICIC_HIRME
Hirudo medicinalis
Eglin C
|
| P00782 |
SUBT_BACAM
Bacillus amyloliquefaciens
Subtilisin BPN'
|
PDB Structure
| PDB | 1SBN |
| External Links | |
| Method | X-RAY DIFFRACTION |
| Organism | Escherichia |
| Primary Citation |
Refined crystal structures of subtilisin novo in complex with wild-type and two mutant eglins. Comparison with other serine proteinase inhibitor complexes.
J.Mol.Biol.
|
