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 tetramer (preferred)
Assembly name:
Caspase-3 complex (preferred)
PDBe Complex ID:
PDB-CPX-154726 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Caspase-3 subunit p17
Molecule details ›
Chain: A
Length: 146 amino acids
Theoretical weight: 16.52 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
Sequence domains: Caspase domain
Structure domains: Rossmann fold
Length: 146 amino acids
Theoretical weight: 16.52 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
- Canonical:
P42574 (Residues: 29-174; Coverage: 53%)
Sequence domains: Caspase domain
Structure domains: Rossmann fold
Caspase-3 subunit p12
Molecule details ›
Chain: B
Length: 93 amino acids
Theoretical weight: 11.02 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
Sequence domains: Caspase domain
Structure domains: Caspase-like
Length: 93 amino acids
Theoretical weight: 11.02 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
- Canonical: P42574 (Residues: 185-277; Coverage: 34%)
Sequence domains: Caspase domain
Structure domains: Caspase-like
