4qu0

X-ray diffraction
1.95Å resolution

Caspase-3 Y195AV266H

Released:
Source organism: Homo sapiens
Primary publication:
Modifying caspase-3 activity by altering allosteric networks.
OpenAccess logo Biochemistry 53 7582-95 (2014)
PMID: 25343534

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 tetramer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-154771 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Caspase-3 Chain: A
Molecule details ›
Chain: A
Length: 278 amino acids
Theoretical weight: 31.74 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: E
Molecule details ›
Chain: E
Length: 6 amino acids
Theoretical weight: 535 Da
Source organism: Homo sapiens
Expression system: Not provided

Ligands and Environments

1 bound ligand:
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 22-BM
Spacegroup: I222
Unit cell:
a: 68.62Å b: 84.496Å c: 96.31Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.149 0.145 0.183
Expression systems:
  • Escherichia coli
  • Not provided