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:
Sequence domains:
Structure analysis Details
Assembly composition:
hetero tetramer (preferred)
Assembly name:
Caspase-2 complex and 14-3-3 protein gamma (preferred)
PDBe Complex ID:
PDB-CPX-154825 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
14-3-3 protein gamma
Molecule details ›
Chains: A, B, C, D, E, F, G, H
Length: 234 amino acids
Theoretical weight: 27 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21(DE3)
UniProt:
Sequence domains: 14-3-3 protein
Structure domains: 14-3-3 domain
Length: 234 amino acids
Theoretical weight: 27 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21(DE3)
UniProt:
- Canonical:
P61981 (Residues: 1-234; Coverage: 95%)
Sequence domains: 14-3-3 protein
Structure domains: 14-3-3 domain
Caspase-2
Molecule details ›
Chains: I, J, K, L, M, N, O, P
Length: 8 amino acids
Theoretical weight: 1.03 KDa
Source organism: Homo sapiens
Expression system: Not provided
UniProt:
Length: 8 amino acids
Theoretical weight: 1.03 KDa
Source organism: Homo sapiens
Expression system: Not provided
UniProt:
- Canonical: P42575 (Residues: 136-143; Coverage: 2%)
