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
Assemblies composition:
Assembly name:
Caspase-2 subunit p18 (preferred)
PDBe Complex ID:
PDB-CPX-154811 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 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
Ligands and Environments
No bound ligands
No modified residues
Experiments and Validation Details
X-ray source:
ALS BEAMLINE 8.3.1
Spacegroup:
P212121
Expression system: Escherichia coli
