PDBe 4jqz

X-ray diffraction
2.89Å resolution

Human procaspase-3, crystal form 2

Released:
Source organism: Homo sapiens
Primary publication:
Structural snapshots reveal distinct mechanisms of procaspase-3 and -7 activation.
Proc. Natl. Acad. Sci. U.S.A. (2013)
PMID: 23650375

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:
homo dimer (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Caspase-3 subunit p17 Chains: A, B
Molecule details ›
Chains: A, B
Length: 247 amino acids
Theoretical weight: 28.32 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: P42574 (Residues: 34-277; Coverage: 88%)
Gene names: CASP3, CPP32
Sequence domains: Caspase domain
Structure domains: Rossmann fold

Ligands and Environments

No bound ligands

No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ALS BEAMLINE 8.3.1
Spacegroup: P212121
Unit cell:
a: 50.256Å b: 54.361Å c: 162.014Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.232 0.229 0.256
Expression system: Escherichia coli BL21(DE3)