PDBe 2k7z

Solution NMR

Solution Structure of the Catalytic Domain of Procaspase-8

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:
monomeric (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Caspase-8 subunit p18 Chain: A
Molecule details ›
Chain: A
Length: 266 amino acids
Theoretical weight: 30.35 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

Ligands and Environments

No bound ligands

No modified residues

Experiments and Validation Details

Entry percentile scores
Chemical shift assignment: 80%
Refinement method: molecular dynamics
Chemical shifts: BMR15932  
Expression system: Escherichia coli