PDBe 1qdu

X-ray diffraction
2.8Å resolution

CRYSTAL STRUCTURE OF THE COMPLEX OF CASPASE-8 WITH THE TRIPEPTIDE KETONE INHIBITOR ZEVD-DCBMK

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 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: 88 amino acids
Theoretical weight: 10.19 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: Q14790 (Residues: 390-477; Coverage: 18%)
Gene names: CASP8, MCH5
Structure domains: Caspase-like
PHQ-GLU-VAL-ASP-DICHLOROMETHYLKETONE INHIBITOR Chains: T, U, V, W, X, Y
Molecule details ›
Chains: T, U, V, W, X, Y
Length: 5 amino acids
Theoretical weight: 546 Da

Ligands and Environments

No bound ligands

No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE BM1A
Spacegroup: C2
Unit cell:
a: 93.9Å b: 206.53Å c: 102.05Å
α: 90° β: 102.3° γ: 90°
R-values:
R R work R free
0.23 0.23 0.302
Expression system: Escherichia coli