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.
UniProtKB Entries (1)
Caspase-3 binds diverse P4 residues in peptides as revealed by crystallography and structural modeling.