Function and Biology Details
Reaction catalysed:
Strict requirement for an Asp residue at position P1 and has a preferred cleavage sequence of Asp-Glu-Val-Asp-|-
Biochemical function:
Biological process:
Cellular component:
- not assigned
Sequence domains:
- Ankyrin repeat
- Peptidase C14A, caspase catalytic domain
- Ankyrin repeat-containing domain superfamily
- Peptidase C14, caspase domain
- Caspase-like domain superfamily
- Peptidase C14, caspase non-catalytic subunit p10
- Peptidase family C14A, cysteine active site
- Peptidase family C14A, His active site
2 more domains
Structure analysis Details
Assembly composition:
hetero hexamer (preferred)
Assembly name:
Caspase-7 complex and unmapped proteins (preferred)
PDBe Complex ID:
PDB-CPX-157244 (preferred)
Entry contents:
3 distinct polypeptide molecules
Macromolecules (3 distinct):
Caspase-7 subunit p20
Molecule details ›
Chains: A, C
Length: 175 amino acids
Theoretical weight: 19.75 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
Sequence domains: Caspase domain
Structure domains: Rossmann fold
Length: 175 amino acids
Theoretical weight: 19.75 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
- Canonical:
P55210 (Residues: 24-198; Coverage: 58%)
Sequence domains: Caspase domain
Structure domains: Rossmann fold
Caspase-7 subunit p11
Molecule details ›
Chains: B, D
Length: 105 amino acids
Theoretical weight: 12.42 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
Sequence domains: Caspase domain
Structure domains: Caspase-like
Length: 105 amino acids
Theoretical weight: 12.42 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
- Canonical: P55210 (Residues: 207-303; Coverage: 32%)
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: Escherichia coli
