X-ray diffraction
1.75Å resolution

Crystal structures of caspase-3 in complex with aza-peptide epoxide inhibitors.

Entry authors: Ganesan R, Jelakovic S, Campbell AJ, Li ZZ, Asgian JL, Powers JC, Grutter MG

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:
  • not assigned
Biological process:
  • not assigned
Cellular component:
  • not assigned

Structure analysis Details

Assembly composition:
hetero hexamer (preferred)
Entry contents:
3 distinct polypeptide molecules
Macromolecules (3 distinct):
Caspase-3 subunit p17 Chain: A
Molecule details ›
Chain: A
Length: 147 amino acids
Theoretical weight: 16.64 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21(DE3)
  • Canonical: P42574 (Residues: 29-175; Coverage: 53%)
Gene names: CASP3, CPP32
Structure domains: Rossmann fold
Caspase-3 subunit p12 Chain: B
Molecule details ›
Chain: B
Length: 103 amino acids
Theoretical weight: 11.98 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
  • Canonical: P42574 (Residues: 176-277; Coverage: 37%)
Gene names: CASP3, CPP32
Structure domains: Caspase-like
Molecule details ›
Chain: I
Length: 5 amino acids
Theoretical weight: 792 Da
Source organism: synthetic construct
Expression system: Not provided

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ENRAF-NONIUS FR591
Spacegroup: I222
Unit cell:
a: 66.784Å b: 83.786Å c: 96.453Å
α: 90° β: 90° γ: 90°
R R work R free
0.165 0.165 0.193
Expression systems:
  • Escherichia coli BL21(DE3)
  • Escherichia coli
  • Not provided