PDBe 4ps0

X-ray diffraction
1.63Å resolution

Caspase-8 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 Chains: A, B
Molecule details ›
Chains: A, B
Length: 285 amino acids
Theoretical weight: 32.72 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
(BAL)LQ(HYP)(1U8) PEPTIDE Chains: C, D
Molecule details ›
Chains: C, D
Length: 5 amino acids
Theoretical weight: 705 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: P21
Unit cell:
a: 50.198Å b: 69.189Å c: 93.143Å
α: 90° β: 102.01° γ: 90°
R-values:
R R work R free
0.154 0.153 0.179
Expression systems:
  • Escherichia coli
  • Not provided