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:
Structure domain:
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 ›
Chains: A, D
Length: 147 amino acids
Theoretical weight: 16.64 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21(DE3)
UniProt:
Sequence domains: Caspase domain
Structure domains: Rossmann fold
Length: 147 amino acids
Theoretical weight: 16.64 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21(DE3)
UniProt:
- Canonical:
P42574 (Residues: 29-175; Coverage: 53%)
Sequence domains: Caspase domain
Structure domains: Rossmann fold
Caspase-3 subunit p12
Molecule details ›
Chains: B, E
Length: 102 amino acids
Theoretical weight: 11.91 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21(DE3)
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 BL21(DE3)
UniProt:
- Canonical: P42574 (Residues: 176-277; Coverage: 37%)
Sequence domains: Caspase domain
Structure domains: Caspase-like
