PDBe 4dcj

X-ray diffraction
1.7Å resolution

Crystal structure of caspase 3, L168D mutant

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

Structure analysis Details

Assembly composition:
hetero trimer (preferred)
Entry contents:
3 distinct polypeptide molecules
Macromolecules (3 distinct):
Caspase-3 subunit p17 Chains: A, D
Molecule details ›
Chains: A, D
Length: 147 amino acids
Theoretical weight: 16.64 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: P42574 (Residues: 29-175; Coverage: 53%)
Gene names: CASP3, CPP32
Structure domains: Rossmann fold
Caspase-3 subunit p12 Chains: B, E
Molecule details ›
Chains: B, E
Length: 108 amino acids
Theoretical weight: 12.74 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: P42574 (Residues: 176-277; Coverage: 37%)
Gene names: CASP3, CPP32
Structure domains: Caspase-like
Caspase Inhibitor AC-DEVD-CHO Chains: C, F
Molecule details ›
Chains: C, F
Length: 5 amino acids
Theoretical weight: 488 Da

Ligands and Environments

No bound ligands

No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: PAL/PLS BEAMLINE 4A
Spacegroup: P21
Unit cell:
a: 49.834Å b: 68.553Å c: 93.811Å
α: 90° β: 101.88° γ: 90°
R-values:
R R work R free
0.194 0.19 0.213
Expression system: Escherichia coli