PDBe 2xyg

X-ray diffraction
1.54Å resolution

Caspase-3:CAS329306

Released:
Source organism: Homo sapiens
Primary publication:
In silico identification and crystal structure validation of caspase-3 inhibitors without a P1 aspartic acid moiety.
Acta Crystallogr. Sect. F Struct. Biol. Cryst. Commun. 67 842-50 (2011)
PMID: 21821879

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:
Biological process:
  • not assigned
Cellular component:
  • not assigned

Structure analysis Details

Assembly composition:
hetero tetramer (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Caspase-3 subunit p12 Chain: B
Molecule details ›
Chain: B
Length: 93 amino acids
Theoretical weight: 11.02 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: P42574 (Residues: 185-277; Coverage: 34%)
Gene names: CASP3, CPP32
Caspase-3 subunit p17 Chain: A
Molecule details ›
Chain: A
Length: 146 amino acids
Theoretical weight: 16.52 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: P42574 (Residues: 29-174; Coverage: 53%)
Gene names: CASP3, CPP32
Structure domains: Rossmann fold

Ligands and Environments

1 bound ligand:

No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SLS BEAMLINE X06SA
Spacegroup: I222
Unit cell:
a: 68.799Å b: 83.538Å c: 96.147Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.179 0.179 0.197
Expression system: Escherichia coli