Function and Biology Details
Reaction catalysed:
Strict requirement for an Asp residue at P1, with 316-asp being essential for proteolytic activity and has a preferred cleavage sequence of Val-Asp-Val-Ala-Asp-|-
Biochemical function:
Biological process:
Cellular component:
- not assigned
Structure analysis Details
Assembly composition:
hetero pentamer (preferred)
Assembly name:
Caspase-2 complex and peptide (preferred)
PDBe Complex ID:
PDB-CPX-154822 (preferred)
Entry contents:
3 distinct polypeptide molecules
Macromolecules (3 distinct):
Caspase-2 subunit p18
Molecule details ›
Chains: A, C
Length: 160 amino acids
Theoretical weight: 18.09 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
Sequence domains: Caspase domain
Structure domains: Rossmann fold
Length: 160 amino acids
Theoretical weight: 18.09 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
- Canonical:
P42575 (Residues: 175-333; Coverage: 35%)
Sequence domains: Caspase domain
Structure domains: Rossmann fold
Caspase-2 subunit p12
Molecule details ›
Chains: B, D
Length: 112 amino acids
Theoretical weight: 12.92 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
Sequence domains: Caspase domain
Structure domains: Caspase-like
Length: 112 amino acids
Theoretical weight: 12.92 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
- Canonical: P42575 (Residues: 349-452; Coverage: 23%)
Sequence domains: Caspase domain
Structure domains: Caspase-like
