PDBe 1qtn

X-ray diffraction
1.2Å resolution

CRYSTAL STRUCTURE OF THE COMPLEX OF CASPASE-8 WITH THE TETRAPEPTIDE INHIBITOR ACE-IETD-ALDEHYDE

Released:

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 hexamer (preferred)
Entry contents:
3 distinct polypeptide molecules
Macromolecules (3 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
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
Structure domains: Caspase-like
ACETYL-ILE-GLU-THR-ASP-ALDEHYDE Chain: C
Molecule details ›
Chain: C
Length: 5 amino acids
Theoretical weight: 489 Da
UniProt:

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: 62.4Å b: 62.4Å c: 129.25Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.166 0.143 0.188
Expression system: Escherichia coli