PDBe 4ehd

X-ray diffraction
1.58Å resolution

Allosteric Modulation of Caspase-3 through Mutagenesis

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
Biological process:
Cellular component:

Structure analysis Details

Assemblies composition:
hetero dimer (preferred)
hetero octamer
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Caspase-3 Chain: A
Molecule details ›
Chain: A
Length: 277 amino acids
Theoretical weight: 31.59 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: 69.333Å b: 84.492Å c: 95.916Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.181 0.18 0.199
Expression systems:
  • Escherichia coli
  • Not provided