PDBe 3edq

X-ray diffraction
1.61Å resolution

Crystal structure of Caspase-3 with inhibitor AC-LDESD-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

Assembly composition:
hetero hexamer (preferred)
Entry contents:
3 distinct polypeptide molecules
Macromolecules (3 distinct):
Caspase-3 subunit p17 Chains: A, C
Molecule details ›
Chains: A, C
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, D
Molecule details ›
Chains: B, D
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
AC-LDESD-CHO peptide Chains: E, F
Molecule details ›
Chains: E, F
Length: 6 amino acids
Theoretical weight: 588 Da

Ligands and Environments

No bound ligands

1 modified residue:

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 22-ID
Spacegroup: P212121
Unit cell:
a: 67.375Å b: 93.562Å c: 97.617Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.215 0.178 0.223
Expression system: Escherichia coli