8jol

Electron Microscopy
3Å resolution

cryo-EM structure of the CED-4/CED-3 holoenzyme

Released:
Source organism: Caenorhabditis elegans
Primary publication:
Structural insights into CED-3 activation.
OpenAccess logo Life Sci Alliance 6 (2023)
PMID: 37402593
Related structures: EMD-36459

Function and Biology Details

Reaction catalysed:
Strict requirement for an Asp residue at position P1 and has a preferred cleavage sequence of Asp-Glu-Val-Asp-|-
Biochemical function:
Cellular component:

Structure analysis Details

Assembly composition:
hetero trimer (preferred)
PDBe Complex ID:
PDB-CPX-219360 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Cell death protein 4 Chains: A, B
Molecule details ›
Chains: A, B
Length: 549 amino acids
Theoretical weight: 62.95 KDa
Source organism: Caenorhabditis elegans
Expression system: Escherichia coli
UniProt:
  • Canonical: P30429 (Residues: 1-571; Coverage: 96%)
  • Best match: P30429-2 (Residues: 1-549)
Gene names: C35D10.9, ced-4
Sequence domains:
Cell death protein 3 Chain: C
Molecule details ›
Chain: C
Length: 503 amino acids
Theoretical weight: 56.69 KDa
Source organism: Caenorhabditis elegans
Expression system: Escherichia coli
UniProt:
  • Canonical: P42573 (Residues: 1-503; Coverage: 100%)
Gene names: C48D1.2, ced-3
Sequence domains:

Ligands and Environments

2 bound ligands:
No modified residues

Experiments and Validation Details

Entry percentile scores
Resolution:
Relevant EMDB volumes: EMD-36459
Expression system: Escherichia coli