Function and Biology Details
Reaction catalysed:
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
Biochemical function:
Biological process:
Cellular component:
- not assigned
Sequence domains:
- Peptidase C14A, caspase catalytic domain
- Peptidase C14, caspase domain
- Caspase-like domain superfamily
- Caspase-related proteases and regulators
- Peptidase C14, caspase non-catalytic subunit p10
- Peptidase family C14A, cysteine active site
- Peptidase family C14A, His active site
- Peptidase C14, p20 domain
1 more domain
Structure analysis Details
Assembly composition:
hetero trimer (preferred)
Assembly name:
Caspase-3 and peptide (preferred)
PDBe Complex ID:
PDB-CPX-154690 (preferred)
Entry contents:
3 distinct polypeptide molecules
Macromolecules (3 distinct):
Ligands and Environments
No bound ligands
No modified residues
Experiments and Validation Details
wwPDB Validation report is not available for this entry.
X-ray source:
PAL/PLS BEAMLINE 4A
Spacegroup:
P21
Expression system: Escherichia coli