PDBe 2h5j

X-ray diffraction
2Å resolution

Crystal strusture of caspase-3 with inhibitor Ac-DMQD-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:
  • 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 Chains: A, C
Molecule details ›
Chains: A, C
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 Chains: B, D
Molecule details ›
Chains: B, D
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-DMQD-Cho Chains: E, F
Molecule details ›
Chains: E, F
Length: 5 amino acids
Theoretical weight: 520 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: P21
Unit cell:
a: 50.15Å b: 69.34Å c: 94.09Å
α: 90° β: 102.37° γ: 90°
R-values:
R R work R free
0.206 0.179 0.269
Expression system: Escherichia coli BL21