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
| 3.4.21.100 |
Sedolisin.
based on mapping to UniProt P42790
Hydrolysis of the B chain of insulin at 13-Glu-|-Ala-14, 15-Leu-|-Tyr-16 and 25-Phe-|-Tyr-26 and angiotensin I at 4-Tyr-|-Ile-5. A good synthetic substrate is Lys-Pro-Ile-Glu-Phe-|-Phe(NO(2))-Arg-Leu.
-!- An enzyme secreted by Pseudomonas sp. No. 101. -!- Optimum pH 4. -!- It is distinguished from EC 3.4.21.101 by its insensitivity to EPNP and from EC 3.4.23.31 by this property and by its unrelated amino- acid sequence. -!- Inhibited by tyrostatin, a peptide aldehyde. -!- Belongs to peptidase family S53. -!- Formerly EC 3.4.23.37.
|
UniProtKB Entries (1)
| P42790 |
PICP_PSESR
Pseudomonas sp. 101
Pseudomonalisin
|
PDB Structure
| PDB | 1GA1 |
| External Links | |
| Method | X-RAY DIFFRACTION |
| Organism | Escherichia |
| Primary Citation |
Practical experience with the use of halides for phasing macromolecular structures: a powerful tool for structural genomics.
Acta Crystallogr.,Sect.D
|
