PDBe 3itn

X-ray diffraction
1.63Å resolution

Crystal structure of Pseudo-activated Procaspase-3

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 octamer
hetero tetramer
hetero dimer (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Caspase-3 subunit p17 Chain: A
Molecule details ›
Chain: A
Length: 250 amino acids
Theoretical weight: 28.63 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: P42574 (Residues: 29-277; Coverage: 90%)
Gene names: CASP3, CPP32
Sequence domains: Caspase domain
Structure domains: Rossmann fold
ACETYL-ASP-GLU-VAL-ASP-CHLOROMETHYL KETONE inhibitor Chain: B
Molecule details ›
Chain: B
Length: 6 amino acids
Theoretical weight: 535 Da
Source organism: Homo sapiens
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: 69.224Å b: 84.607Å c: 96.171Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.22 0.199 0.224
Expression systems:
  • Escherichia coli
  • Not provided