PDBe 1f9e

X-ray diffraction
2.9Å resolution

CASPASE-8 SPECIFICITY PROBED AT SUBSITE S4: CRYSTAL STRUCTURE OF THE CASPASE-8-Z-DEVD-CHO

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:
  • not assigned
Biological process:
  • not assigned
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 Chains: A, C, E, G, I, K
Molecule details ›
Chains: A, C, E, G, I, K
Length: 153 amino acids
Theoretical weight: 17.42 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: Q14790 (Residues: 222-374; Coverage: 32%)
Gene names: CASP8, MCH5
Structure domains: Rossmann fold
Caspase-8 subunit p10 Chains: B, D, F, H, J, L
Molecule details ›
Chains: B, D, F, H, J, L
Length: 89 amino acids
Theoretical weight: 10.27 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: Q14790 (Residues: 390-478; Coverage: 19%)
Gene names: CASP8, MCH5
Structure domains: Caspase-like
(PHQ)DEVD Chains: Q, R, S, T, U, V
Molecule details ›
Chains: Q, R, S, T, U, V
Length: 5 amino acids
Theoretical weight: 613 Da

Ligands and Environments

No bound ligands

1 modified residue:

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE ID14-1
Spacegroup: C2221
Unit cell:
a: 98.029Å b: 188.748Å c: 209.802Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.241 0.241 0.289
Expression system: Escherichia coli