CATH Classification
| Level | CATH Code | Description |
|---|---|---|
|
3 | Alpha Beta |
|
3.90 | Alpha-Beta Complex |
|
3.90.226 | 2-enoyl-CoA Hydratase; Chain A, domain 1 |
|
3.90.226.10 | 2-enoyl-CoA Hydratase; Chain A, domain 1 |
Domain Context
CATH Clusters
| Superfamily | 2-enoyl-CoA Hydratase; Chain A, domain 1 |
| Functional Family | ATP-dependent Clp protease proteolytic subunit |
Enzyme Information
| 3.4.21.92 |
Endopeptidase Clp.
based on mapping to UniProt P63788
Hydrolysis of proteins to small peptides in the presence of ATP and magnesium. Alpha-casein is the usual test substrate. In the absence of ATP, only oligopeptides shorter than five residues are hydrolyzed (such as succinyl-Leu-Tyr-|-NHMec, and Leu-Tyr-Leu-|-Tyr-Trp, in which cleavage of the -Tyr-|-Leu- and -Tyr-|-Trp bonds also occurs).
-!- Belongs to peptidase family S14.
|
UniProtKB Entries (1)
| P63788 |
CLPP_STRR6
Streptococcus pneumoniae R6
ATP-dependent Clp protease proteolytic subunit
|
PDB Structure
| PDB | 1Y7O |
| External Links | |
| Method | X-RAY DIFFRACTION |
| Organism | Escherichia |
| Primary Citation |
The ClpP double ring tetradecameric protease exhibits plastic ring-ring interactions, and the N termini of its subunits form flexible loops that are essential for ClpXP and ClpAP complex formation.
J.Biol.Chem.
|