PDBe 4que

X-ray diffraction
1.84Å resolution

Caspase-3 Y195FV266H

Released:
Source organism: Homo sapiens

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 hexamer (preferred)
Entry contents:
3 distinct polypeptide molecules
Macromolecules (3 distinct):
Caspase-3 Chains: A, C
Molecule details ›
Chains: A, C
Length: 277 amino acids
Theoretical weight: 31.67 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 Chains: H, J
Molecule details ›
Chains: H, J
Length: 6 amino acids
Theoretical weight: 535 Da
Source organism: Homo sapiens
Expression system: Not provided
SHORT PEPTIDE Chains: D, E
Molecule details ›
Chains: D, E
Length: 5 amino acids
Theoretical weight: 594 Da
Source organism: Homo sapiens
Expression system: Not provided

Ligands and Environments

2 bound ligands:

No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 22-ID
Spacegroup: C2
Unit cell:
a: 109.125Å b: 96.362Å c: 68.833Å
α: 90° β: 127.1° γ: 90°
R-values:
R R work R free
0.182 0.18 0.223
Expression systems:
  • Escherichia coli
  • Not provided