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
Structure analysis Details
Assembly composition:
hetero trimer (preferred)
Assembly name:
Caspase-3 and peptide (preferred)
PDBe Complex ID:
PDB-CPX-154698 (preferred)
Entry contents:
3 distinct polypeptide molecules
Macromolecules (3 distinct):
Caspase-3 subunit p17
Molecule details ›
Chains: A, B
Length: 175 amino acids
Theoretical weight: 19.7 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli K-12
UniProt:
Sequence domains: Caspase domain
Structure domains: Rossmann fold
Length: 175 amino acids
Theoretical weight: 19.7 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli K-12
UniProt:
- Canonical:
P42574 (Residues: 1-175; Coverage: 63%)
Sequence domains: Caspase domain
Structure domains: Rossmann fold
Caspase-3 subunit p12
Molecule details ›
Chains: C, D
Length: 102 amino acids
Theoretical weight: 11.91 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli K-12
UniProt:
Sequence domains: Caspase domain
Structure domains: Caspase-like
Length: 102 amino acids
Theoretical weight: 11.91 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli K-12
UniProt:
- Canonical: P42574 (Residues: 176-277; Coverage: 37%)
Sequence domains: Caspase domain
Structure domains: Caspase-like
