CATH Classification
| Level | CATH Code | Description |
|---|---|---|
|
3 | Alpha Beta |
|
3.20 | Alpha-Beta Barrel |
|
3.20.20 | TIM Barrel |
|
3.20.20.140 | Metal-dependent hydrolases |
Domain Context
CATH Clusters
| Superfamily | Metal-dependent hydrolases |
| Functional Family | Dipeptidase gliJ |
Enzyme Information
| 3.4.13.19 |
Membrane dipeptidase.
based on mapping to UniProt Q4WMJ8
Hydrolysis of dipeptides.
-!- Membrane bound, with broad specificity. -!- Abundant in the kidney cortex. -!- Inhibited by bestatin and cilastatin. -!- Belongs to peptidase family M19. -!- Formerly EC 3.4.3.1, EC 3.4.3.2, EC 3.4.3.6, EC 3.4.13.1, EC 3.4.13.2, EC 3.4.13.8, EC 3.4.13.11 and EC 3.4.13.15.
|
UniProtKB Entries (1)
| Q4WMJ8 |
GLIJ_ASPFU
Aspergillus fumigatus Af293
Dipeptidase gliJ
|
PDB Structure
| PDB | 5LX7 |
| External Links | |
| Method | X-RAY DIFFRACTION |
| Organism | |
| Primary Citation |
Gliotoxin Biosynthesis: Structure, Mechanism, and Metal Promiscuity of Carboxypeptidase GliJ.
ACS Chem. Biol.
|