CATH Classification
| Level | CATH Code | Description |
|---|---|---|
|
3 | Alpha Beta |
|
3.30 | 2-Layer Sandwich |
|
3.30.70 | Alpha-Beta Plaits |
|
3.30.70.1470 | Caspase-like |
Domain Context
CATH Clusters
| Superfamily | Caspase-like |
| Functional Family | Caspase-3 |
Enzyme Information
| 3.4.22.60 |
Caspase-7.
based on mapping to UniProt P55210
Strict requirement for an Asp residue at position P1 and has a preferred cleavage sequence of Asp-Glu-Val-Asp-|-.
-!- Caspase-7 is an effector/executioner caspase, as are caspase-3 (EC 3.4.22.56) and caspase-6 (EC 3.4.22.59). -!- These caspases are responsible for the proteolysis of the majority of cellular polypeptides, (e.g. poly(ADP-ribose) polymerase (PARP)), which lead to the apoptotic phenotype. -!- Although a hydrophobic residue at P5 of caspase-2 (EC 3.4.22.55) and caspase-3 leads to more efficient hydrolysis, the amino-acid residue at this location in caspase-7 has no effect. -!- Caspase-7 is activated by the initiator caspases (caspase-8 (EC 3.4.22.61), caspase-9 (EC 3.4.22.62) and caspase-10 (EC 3.4.22.63)). -!- Removal of the N-terminal prodomain occurs before cleavage in the linker region between the large and small subunits. -!- Belongs to peptidase family C14.
|
UniProtKB Entries (1)
| P55210 |
CASP7_HUMAN
Homo sapiens
Caspase-7
|
PDB Structure
| PDB | 2QL9 |
| External Links | |
| Method | X-RAY DIFFRACTION |
| Organism | Escherichia |
| Primary Citation |
Plasticity of S2-S4 specificity pockets of executioner caspase-7 revealed by structural and kinetic analysis.
Febs J.
|
