PDBe 2h5i

X-ray diffraction
1.69Å resolution

Crystal structure of caspase-3 with 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

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 BL21
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: 95 amino acids
Theoretical weight: 11.26 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21
UniProt:
  • Canonical: P42574 (Residues: 184-277; Coverage: 34%)
Gene names: CASP3, CPP32
Structure domains: Caspase-like
Ac-DEV(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: APS BEAMLINE 22-ID
Spacegroup: I222
Unit cell:
a: 69.92Å b: 86.05Å c: 97.99Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.186 0.184 0.227
Expression system: Escherichia coli BL21