CATH Classification

Domain Context

CATH Clusters

Superfamily Caspase-like
Functional Family Caspase-3

Enzyme Information
based on mapping to UniProt P42574
Strict requirement for an Asp residue at positions P1 and P4. It has a preferred cleavage sequence of Asp-Xaa-Xaa-Asp-|- with a hydrophobic amino-acid residue at P2 and a hydrophilic amino-acid residue at P3, although Val or Ala are also accepted at this position.
-!- Caspase-3 is an effector/executioner caspase, as are caspase-6 (EC and caspase-7 (EC -!- These caspases are responsible for the proteolysis of the majority of cellular polypeptides, (e.g. poly(ADP-ribose) polymerase (PARP)), which leads to the apoptotic phenotype. -!- Procaspase-3 can be activated by caspase-1 (EC, caspase-8 (EC, caspase-9 (EC and caspase-10 (EC as well as by the serine protease granzyme B. -!- Caspase-3 can activate procaspase-2 (EC -!- Activation occurs by inter-domain cleavage followed by removal of the N-terminal prodomain. -!- While Asp-Glu-(Val/Ile)-Asp is thought to be the preferred cleavage sequence, the enzyme can accommodate different residues at P2 and P3 of the substrate. -!- Like caspase-2, a hydrophobic residue at P5 of caspase-3 leads to more efficient hydrolysis, e.g. (Val/Leu)-Asp-Val-Ala-Asp-|- is a better substrate than Asp-Val-Ala-Asp-|-. -!- This is not the case for caspase-7. -!- Belongs to peptidase family C14.

UniProtKB Entries (1)

Homo sapiens

PDB Structure

External Links
Primary Citation
Specific Inhibition of Caspase-3 by a Competitive Darpin: Molecular Mimicry between Native and Designed Inhibitors.
Schroeder, T., Barandun, J., Flutsch, A., Briand, C., Mittl, P., Grutter, M.G.