Function and Biology Details
Reaction catalysed:
Strict requirement for Asp at position P1 and has a preferred cleavage sequence of Val-Glu-His-Asp-|-
Biochemical function:
Biological process:
Cellular component:
- not assigned
Structure analysis Details
Assemblies composition:
Assembly name:
Caspase-6 and peptide (preferred)
PDBe Complex ID:
PDB-CPX-157272 (preferred)
Entry contents:
3 distinct polypeptide molecules
Macromolecules (3 distinct):
Caspase-6 subunit p18
Molecule details ›
Chains: A, C, E, G
Length: 156 amino acids
Theoretical weight: 18.1 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
Sequence domains: Caspase domain
Structure domains: Rossmann fold
Length: 156 amino acids
Theoretical weight: 18.1 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
- Canonical:
P55212 (Residues: 24-179; Coverage: 53%)
Sequence domains: Caspase domain
Structure domains: Rossmann fold
Caspase-6 subunit p11
Molecule details ›
Chains: B, D, F, H
Length: 100 amino acids
Theoretical weight: 11.3 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
Sequence domains: Caspase domain
Structure domains: Caspase-like
Length: 100 amino acids
Theoretical weight: 11.3 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
- Canonical: P55212 (Residues: 194-293; Coverage: 34%)
Sequence domains: Caspase domain
Structure domains: Caspase-like
Ligands and Environments
No bound ligands
No modified residues
Experiments and Validation Details
X-ray source:
DIAMOND BEAMLINE I04
Spacegroup:
P21
Expression systems:
- Escherichia coli
- Not provided
