PDBe 2dko

X-ray diffraction
1.06Å resolution

Extended substrate recognition in caspase-3 revealed by high resolution X-ray structure analysis

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:
Biological process:
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: 146 amino acids
Theoretical weight: 16.52 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: P42574 (Residues: 29-174; 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
UniProt:
  • Canonical: P42574 (Residues: 176-277; Coverage: 37%)
Gene names: CASP3, CPP32
Structure domains: Caspase-like
PHQ-ASP-GLU-VAL-ASP-CHLOROMETHYLKETONE Chain: I
Molecule details ›
Chain: I
Length: 6 amino acids
Theoretical weight: 661 Da

Ligands and Environments

No bound ligands

No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SLS BEAMLINE X06SA
Spacegroup: I222
Unit cell:
a: 67.65Å b: 83.89Å c: 96.16Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.142 0.142 0.175
Expression system: Escherichia coli