PDBe 3h11

X-ray diffraction
1.9Å resolution

Zymogen caspase-8:c-FLIPL protease domain complex

Released:
Source organism: Homo sapiens
Primary publication:
Mechanism of procaspase-8 activation by c-FLIPL.
Proc. Natl. Acad. Sci. U.S.A. 106 8169-74 (2009)
PMID: 19416807

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 trimer (preferred)
Entry contents:
3 distinct polypeptide molecules
Macromolecules (3 distinct):
CASP8 and FADD-like apoptosis regulator subunit p43 Chain: A
Molecule details ›
Chain: A
Length: 272 amino acids
Theoretical weight: 31.45 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: O15519 (Residues: 209-480; Coverage: 57%)
  • Best match: O15519-10 (Residues: 209-265)
Gene names: CASH, CASP8AP1, CFLAR, CLARP, MRIT
Sequence domains: Caspase domain
Structure domains: Rossmann fold
Caspase-8 subunit p18 Chain: B
Molecule details ›
Chain: B
Length: 271 amino acids
Theoretical weight: 31 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: Q14790 (Residues: 217-479; Coverage: 55%)
Gene names: CASP8, MCH5
Sequence domains: Caspase domain
Structure domains: Rossmann fold
IETD aldehyde inhibitor Chain: C
Molecule details ›
Chain: C
Length: 5 amino acids
Theoretical weight: 532 Da

Ligands and Environments

No bound ligands

1 modified residue:

Experiments and Validation Details

Entry percentile scores
X-ray source: NSLS BEAMLINE X29A
Spacegroup: P212121
Unit cell:
a: 52.99Å b: 76.68Å c: 114.19Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.212 0.212 0.25
Expression system: Escherichia coli