CATH Classification
Level | CATH Code | Description |
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3 | Alpha Beta |
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3.30 | 2-Layer Sandwich |
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3.30.70 | Alpha-Beta Plaits |
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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.
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UniProtKB Entries (1)
P55210 |
CASP7_HUMAN
Homo sapiens
Caspase-7
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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.
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