4ehn

X-ray diffraction
1.69Å resolution

Allosteric Modulation of Caspase-3 through Mutagenesis

Released:
Primary publication:
Allosteric modulation of caspase 3 through mutagenesis.
OpenAccess logo Biosci Rep 32 401-11 (2012)
PMID: 22607239

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

Structure analysis Details

Assemblies composition:
hetero dimer (preferred)
hetero tetramer
Assembly name:
PDBe Complex ID:
PDB-CPX-154720 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Caspase-3 Chain: A
Molecule details ›
Chain: A
Length: 277 amino acids
Theoretical weight: 31.57 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: P42574 (Residues: 1-277; Coverage: 100%)
Gene names: CASP3, CPP32
Sequence domains: Caspase domain
Structure domains: Rossmann fold
ACE-ASP-GLU-VAL-ASP-CHLOROMETHYLKETONE INHIBITOR Chain: B
Molecule details ›
Chain: B
Length: 6 amino acids
Theoretical weight: 535 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: APS BEAMLINE 22-ID
Spacegroup: I222
Unit cell:
a: 68.89Å b: 85.522Å c: 96.341Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.192 0.16 0.192
Expression systems:
  • Escherichia coli
  • Not provided