› 2k7z

Solution NMR

Solution Structure of the Catalytic Domain of Procaspase-8

Released:
DOI: 10.2210/pdb2k7z/pdb
PDB entry 2k7z coloured by chain, ensemble of 20 models, front view.
PDB entry 2k7z coloured by chain, ensemble of 20 models, side view.
PDB entry 2k7z coloured by chain, ensemble of 20 models, top view.
Source organism: Homo sapiens
Primary publication:
Structural and biochemical studies on procaspase-8: new insights on initiator caspase activation.
Keller N, Mares J, Zerbe O, Grütter MG
Structure 17 438-48 (2009)
PMID: 19278658

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:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-172099 (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: 82%
Refinement method: molecular dynamics
Expression system: Escherichia coli

Quick links

Citations

7 review citations

Regulated cell death: signaling and mechanisms.
Ashkenazi et al. (2014)
6 more

16 mentions without citation

A primer on caspase mechanisms.
Ramirez et al. (2018)
15 more