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
Sequence domains:
Structure analysis Details
Assembly composition:
hetero hexamer (preferred)
Assembly name:
Caspase-2 complex and unmapped proteins (preferred)
PDBe Complex ID:
PDB-CPX-154818 (preferred)
Entry contents:
3 distinct polypeptide molecules
Macromolecules (3 distinct):
Caspase-2 subunit p18
Molecule details ›
Chains: A, C, E, G, I, K
Length: 169 amino acids
Theoretical weight: 19.01 KDa
Source organism: Homo sapiens
UniProt:
Sequence domains: Caspase domain
Structure domains: Rossmann fold
Length: 169 amino acids
Theoretical weight: 19.01 KDa
Source organism: Homo sapiens
UniProt:
- Canonical:
P42575 (Residues: 167-333; Coverage: 37%)
Sequence domains: Caspase domain
Structure domains: Rossmann fold
Caspase-2 subunit p12
Molecule details ›
Chains: B, D, F, H, J, L
Length: 106 amino acids
Theoretical weight: 12.05 KDa
Source organism: Homo sapiens
Expression system: Not provided
UniProt:
Sequence domains: Caspase domain
Structure domains: Caspase-like
Length: 106 amino acids
Theoretical weight: 12.05 KDa
Source organism: Homo sapiens
Expression system: Not provided
UniProt:
- Canonical: P42575 (Residues: 348-452; Coverage: 23%)
Sequence domains: Caspase domain
Structure domains: Caspase-like
Ligands and Environments
No bound ligands
No modified residues
Experiments and Validation Details
X-ray source:
SLS BEAMLINE X06SA
Spacegroup:
P21
Expression system: Not provided
