CATH Classification
| Level | CATH Code | Description |
|---|---|---|
|
1 | Mainly Alpha |
|
1.10 | Orthogonal Bundle |
|
1.10.390 | Neutral Protease; domain 2 |
|
1.10.390.10 | Neutral Protease Domain 2 |
Domain Context
CATH Clusters
| Superfamily | Neutral Protease Domain 2 |
| Functional Family | Thermolysin |
Enzyme Information
| 3.4.24.27 |
Thermolysin.
based on mapping to UniProt P00800
Preferential cleavage: Xaa-|-Leu > Xaa-|-Phe.
-!- A thermostable extracellular metalloendopeptidase containing four calcium ions. -!- Enzymes that may be species variants of thermolysin are reported from Micrococcus caseolyticus and Aspergillus oryzae. -!- Closely related but distinct enzymes are aeromonolysin, pseudolysin, bacillolysin, aureolysin and mycolysin. -!- Belongs to peptidase family M4. -!- Formerly EC 3.4.24.4.
|
UniProtKB Entries (1)
| P00800 |
THER_BACTH
Bacillus thermoproteolyticus
Thermolysin
|
PDB Structure
| PDB | 1OS0 |
| External Links | |
| Method | X-RAY DIFFRACTION |
| Organism | |
| Primary Citation |
Interactions of a new alpha-aminophosphinic derivative inside the active site of TLN (thermolysin): a model for zinc-metalloendopeptidase inhibition.
Acta Crystallogr.,Sect.D
|