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 Q9JZ38
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)
Q9JZ38 |
CLPP_NEIMB
Neisseria meningitidis MC58
ATP-dependent Clp protease proteolytic subunit
|
PDB Structure
PDB | 5DKP |
External Links | |
Method | X-RAY DIFFRACTION |
Organism | |
Primary Citation |
Development and Characterization of Potent Cyclic Acyldepsipeptide Analogues with Increased Antimicrobial Activity.
J.Med.Chem.
|