1i4e

X-ray diffraction
3Å resolution

CRYSTAL STRUCTURE OF THE CASPASE-8/P35 COMPLEX

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

Assemblies composition:
hetero dimer (preferred)
hetero tetramer
PDBe Complex ID:
PDB-CPX-139942 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Early 35 kDa protein Chain: A
Molecule details ›
Chain: A
Length: 299 amino acids
Theoretical weight: 34.77 KDa
Source organism: Autographa californica nucleopolyhedrovirus
Expression system: Escherichia coli
UniProt:
  • Canonical: P08160 (Residues: 2-299; Coverage: 100%)
Gene name: P35
Sequence domains: Apoptosis preventing protein
Structure domains: Baculovirus p35
Caspase-8 subunit p18 Chain: B
Molecule details ›
Chain: B
Length: 258 amino acids
Theoretical weight: 29.52 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: Q14790 (Residues: 222-479; Coverage: 54%)
Gene names: CASP8, MCH5
Sequence domains: Caspase domain
Structure domains: Rossmann fold

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 32-ID
Spacegroup: C2221
Unit cell:
a: 99.97Å b: 117.34Å c: 346.45Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.236 0.236 0.296
Expression system: Escherichia coli