7xn4

Electron Microscopy
3.35Å resolution

Cryo-EM structure of CopC-CaM-caspase-3 with NAD+

Released:

Function and Biology Details

Reaction catalysed:
Strict requirement for an Asp residue at positions P1 and P4. It has a preferred cleavage sequence of Asp-Xaa-Xaa-Asp-|- with a hydrophobic amino-acid residue at P2 and a hydrophilic amino-acid residue at P3, although Val or Ala are also accepted at this position
Biochemical function:
Cellular component:

Structure analysis Details

Assembly composition:
hetero tetramer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-534417 (preferred)
Entry contents:
3 distinct polypeptide molecules
Macromolecules (3 distinct):
Caspase-3 Chains: A, C
Molecule details ›
Chains: A, C
Length: 277 amino acids
Theoretical weight: 31.65 KDa
Source organism: Homo sapiens
Expression system: Bacteria Latreille et al. 1825
UniProt:
  • Canonical: P42574 (Residues: 1-277; Coverage: 100%)
Gene names: CASP3, CPP32
Sequence domains: Caspase domain
Arginine ADP-riboxanase CopC Chain: B
Molecule details ›
Chain: B
Length: 487 amino acids
Theoretical weight: 52.99 KDa
Source organism: Chromobacterium violaceum
Expression system: Bacteria Latreille et al. 1825
UniProt:
  • Canonical: Q7NWF2 (Residues: 1-487; Coverage: 100%)
Gene names: CV_2038, copC
Sequence domains:
Calmodulin-1 Chain: D
Molecule details ›
Chain: D
Length: 149 amino acids
Theoretical weight: 16.85 KDa
Source organism: Homo sapiens
Expression system: Bacteria Latreille et al. 1825
UniProt:
  • Canonical: P0DP23 (Residues: 1-149; Coverage: 100%)
Gene names: CALM, CALM1, CAM, CAM1
Sequence domains: EF-hand domain pair

Ligands and Environments

1 bound ligand:
No modified residues

Experiments and Validation Details

Entry percentile scores
Resolution: 3.35Å
Relevant EMDB volumes: EMD-33310
Expression system: Bacteria Latreille et al. 1825