PDBe 2cjy

X-ray diffraction
1.67Å 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:
  • 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)
UniProt:
  • 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 BL21(DE3)
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
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: 67.468Å b: 83.834Å c: 96.176Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.176 0.176 0.206
Expression systems:
  • Escherichia coli BL21(DE3)
  • Not provided