PDBe 4zbw

X-ray diffraction
2.2Å resolution

Crystal structure of death effector domain of Caspase8 in Homo Sapiens

Released:
Source organism: Homo sapiens
Primary publication:
Crystal structure of the death effector domains of caspase-8.
Biochem. Biophys. Res. Commun. 463 297-302 (2015)
PMID: 26003730

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:
homo dimer (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Caspase-8 Chains: A, B
Molecule details ›
Chains: A, B
Length: 190 amino acids
Theoretical weight: 22.49 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: Q14790 (Residues: 2-188; Coverage: 39%)
Gene names: CASP8, MCH5
Sequence domains: Death effector domain
Structure domains: Death Domain, Fas

Ligands and Environments

No bound ligands

No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU MICROMAX-002+
Spacegroup: P1
Unit cell:
a: 51.36Å b: 52.106Å c: 56.596Å
α: 113.34° β: 116.89° γ: 90.12°
R-values:
R R work R free
0.208 0.204 0.251
Expression system: Escherichia coli