PDBe 1pau

X-ray diffraction
2.5Å resolution

Crystal structure of the complex of apopain with the tetrapeptide aldehyde inhibitor AC-DEVD-CHO

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

Assemblies composition:
hetero trimer (preferred)
hetero 12-mer
hetero hexamer
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
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: 102 amino acids
Theoretical weight: 11.91 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
ACE-ASP-GLU-VAL-ASJ Chain: C
Molecule details ›
Chain: C
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: RIGAKU RUH2R
Spacegroup: I222
Unit cell:
a: 69.81Å b: 84.62Å c: 96.79Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.195 0.195 0.275
Expression system: Escherichia coli