PDBe 1qx3

X-ray diffraction
1.9Å resolution

Conformational restrictions in the active site of unliganded human caspase-3

Released:
Source organism: Homo sapiens
Primary publication:
Conformational restrictions in the active site of unliganded human caspase-3.
J. Mol. Recognit. 16 121-4
PMID: 12833566

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

Assembly composition:
homo dimer (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Caspase-3 subunit p17 Chain: A
Molecule details ›
Chain: A
Length: 257 amino acids
Theoretical weight: 29.59 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21
UniProt:
  • Canonical: P42574 (Residues: 29-277; Coverage: 90%)
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: SSRL BEAMLINE BL7-1
Spacegroup: P21212
Unit cell:
a: 70.26Å b: 96.19Å c: 44.17Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.249 0.249 0.278
Expression system: Escherichia coli BL21