PDBe 3dek

X-ray diffraction
2.4Å resolution

Crystal Structures of Caspase-3 with Bound Isoquinoline-1,3,4-trione Derivative Inhibitors

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
Biological process:
Cellular component:

Structure analysis Details

Assemblies composition:
homo dimer (preferred)
homo tetramer
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Caspase-3 subunit p17 Chains: A, B, C, D
Molecule details ›
Chains: A, B, C, D
Length: 249 amino acids
Theoretical weight: 28.57 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: P42574 (Residues: 29-277; Coverage: 90%)
Gene names: CASP3, CPP32
Sequence domains: Caspase domain
Structure domains: Rossmann fold

Ligands and Environments

1 bound ligand:

1 modified residue:

Experiments and Validation Details

Entry percentile scores
X-ray source: PHOTON FACTORY BEAMLINE BL-17A
Spacegroup: P212121
Unit cell:
a: 65.17Å b: 96.311Å c: 180.235Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.212 0.209 0.253
Expression system: Escherichia coli BL21(DE3)