PDBe 4jje

X-ray diffraction
1.48Å resolution

Caspase-3 specific unnatural amino acid peptides

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
Biological process:
Cellular component:

Structure analysis Details

Assembly composition:
hetero dimer (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Caspase-3 subunit p17 Chain: A
Molecule details ›
Chain: A
Length: 257 amino acids
Theoretical weight: 29.6 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: P42574 (Residues: 29-277; Coverage: 90%)
Gene names: CASP3, CPP32
Sequence domains: Caspase domain
Structure domains: Rossmann fold
Caspase inhibitor Chain: B
Molecule details ›
Chain: B
Length: 6 amino acids
Theoretical weight: 823 Da
Source organism: Homo sapiens
Expression system: Not provided

Ligands and Environments

No bound ligands

1 modified residue:

Experiments and Validation Details

Entry percentile scores
X-ray source: SSRL BEAMLINE BL11-1
Spacegroup: I222
Unit cell:
a: 68.11Å b: 84.334Å c: 96.088Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.151 0.15 0.174
Expression systems:
  • Escherichia coli BL21(DE3)
  • Not provided