5iag

X-ray diffraction
1.98Å resolution

Caspase 3 V266Q

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

Structure analysis Details

Assembly composition:
hetero trimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-154724 (preferred)
Entry contents:
3 distinct polypeptide molecules
Macromolecules (3 distinct):
Caspase-3 Chain: A
Molecule details ›
Chain: A
Length: 277 amino acids
Theoretical weight: 31.68 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-ASK Chain: B
Molecule details ›
Chain: B
Length: 6 amino acids
Theoretical weight: 535 Da
Source organism: unidentified
ASP-ASP-ASP-MET Chain: D
Molecule details ›
Chain: D
Length: 4 amino acids
Theoretical weight: 494 Da
Source organism: unidentified
Expression system: Escherichia coli

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: 69.04Å b: 85.104Å c: 96.273Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.164 0.159 0.216
Expression system: Escherichia coli