› 5h33

X-ray diffraction
3.6Å resolution

Structural basis for dimerization of the death effector domains of Caspase-8

Released:
DOI: 10.2210/pdb5h33/pdb
PDB entry 5h33 coloured by chain, front view.
PDB entry 5h33 coloured by chain, side view.
PDB entry 5h33 coloured by chain, top view.
Source organism: Homo sapiens
Entry authors: Shen C, Pei J, Guo X, Quan J

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
Sequence domains:

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-172100 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Caspase-8 Chains: A, B
Molecule details ›
Chains: A, B
Length: 188 amino acids
Theoretical weight: 22.34 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: Q14790 (Residues: 1-188; Coverage: 39%)
Gene names: CASP8, MCH5
Sequence domains: Death effector domain

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU MICROMAX-002+
Spacegroup: P21
Unit cell:
a: 56.42Å b: 50.94Å c: 90.444Å
α: 90° β: 105.236° γ: 90°
R-values:
R R work R free
0.283 0.28 0.313
Expression system: Escherichia coli

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