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CRYSTAL STRUCTURE OF THE COMPLEX OF CASPASE-3 WITH A 5,6,7 TRICYCLIC PEPTIDOMIMETIC INHIBITOR

X-ray diffraction
2.51Å resolution
PDB entry 1rhu coloured by chain, front view.
PDB entry 1rhu coloured by chain, side view.
PDB entry 1rhu coloured by chain, top view.
Source organism: Homo sapiens
Assembly composition:
hetero tetramer (preferred)
Entry contents: 2 distinct polypeptide molecules

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Assemblies

Assembly 1 (preferred)
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Assembly Name: Caspase-3 complex
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Multimeric state: hetero tetramer
Accessible surface area: 17217.35 Å2
Buried surface area: 15379.41 Å2
Dissociation area: 2,300.45 Å2
Dissociation energy (ΔGdiss): 20.35 kcal/mol
Dissociation entropy (TΔSdiss): 13.39 kcal/mol
Symmetry number: 2
PDBe Complex ID: PDB-CPX-154726
Complex Portal ID: CPX-970

Macromolecules

Caspase-3 subunit p17
Chain: A
Length: 147 amino acids
Theoretical weight: 16.64 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: P42574 (Residues: 29-175; Coverage: 53%)
Gene names: CASP3, CPP32
Pfam: Caspase domain
InterPro:
CATH: Rossmann fold
SCOP: Caspase catalytic domain
Caspase-3 subunit p17 in PDB entry 1rhu, assembly 1, front view.
Caspase-3 subunit p17 in PDB entry 1rhu, assembly 1, side view.
Caspase-3 subunit p17 in PDB entry 1rhu, assembly 1, top view.
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Caspase-3 subunit p12
Chain: B
Length: 102 amino acids
Theoretical weight: 11.91 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: P42574 (Residues: 176-277; Coverage: 37%)
Gene names: CASP3, CPP32
Pfam: Caspase domain
InterPro:
CATH: Caspase-like
SCOP: Caspase catalytic domain
Caspase-3 subunit p12 in PDB entry 1rhu, assembly 1, front view.
Caspase-3 subunit p12 in PDB entry 1rhu, assembly 1, side view.
Caspase-3 subunit p12 in PDB entry 1rhu, assembly 1, top view.
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