CATH Classification
| Level | CATH Code | Description |
|---|---|---|
|
3 | Alpha Beta |
|
3.90 | Alpha-Beta Complex |
|
3.90.70 | Cathepsin B; Chain A |
|
3.90.70.10 | Cysteine proteinases |
Domain Context
CATH Clusters
| Superfamily | Cysteine proteinases |
| Functional Family | Calpain-1 catalytic subunit |
Enzyme Information
| 3.4.22.52 |
Calpain-1.
based on mapping to UniProt P97571
Broad endopeptidase specificity.
-!- Cytosolic in animal cells. -!- The active enzyme molecule is a heterodimer in which the large subunit contains the peptidase unit, and the small subunit is also a component of EC 3.4.22.53. -!- Belongs to peptidase family C2. -!- Formerly EC 3.4.22.17 and EC 3.4.24.5.
|
| 3.4.22.53 |
Calpain-2.
based on mapping to UniProt Q07009
Broad endopeptidase specificity.
-!- Cytosolic in animal cells. -!- The active enzyme molecule is a heterodimer in which the large subunit contains the peptidase unit, and the small subunit is also a component of EC 3.4.22.52. -!- Belongs to peptidase family C2. -!- Formerly EC 3.4.22.17 and EC 3.4.24.5.
|
UniProtKB Entries (1)
| Q07009 |
CAN2_RAT
Rattus norvegicus
Calpain-2 catalytic subunit
|
PDB Structure
| PDB | 1QXP |
| External Links | |
| Method | X-RAY DIFFRACTION |
| Organism | Escherichia |
| Primary Citation |
Crystal Structure of a mu-like calpain reveals a partially activated conformation with low Ca(2+) requirement
Structure
|
