3kjq

X-ray diffraction
1.8Å resolution

Function and Biology Details

Reaction catalysed:
Strict requirement for Asp at position P1 and has a preferred cleavage sequence of (Leu/Asp/Val)-Glu-Thr-Asp-|-(Gly/Ser/Ala)
Biochemical function:
Biological process:
Cellular component:
  • not assigned

Structure analysis Details

Assembly composition:
hetero tetramer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-172101 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Caspase-8 subunit p18 Chain: A
Molecule details ›
Chain: A
Length: 164 amino acids
Theoretical weight: 18.64 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: Q14790 (Residues: 211-374; Coverage: 34%)
Gene names: CASP8, MCH5
Sequence domains: Caspase domain
Structure domains: Rossmann fold
Caspase-8 subunit p10 Chain: B
Molecule details ›
Chain: B
Length: 95 amino acids
Theoretical weight: 10.9 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: Q14790 (Residues: 385-479; Coverage: 20%)
Gene names: CASP8, MCH5
Sequence domains: Caspase domain
Structure domains: Caspase-like

Ligands and Environments

1 bound ligand:
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 17-ID
Spacegroup: P3121
Unit cell:
a: 63.974Å b: 63.974Å c: 130.847Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.185 0.182 0.207
Expression system: Escherichia coli