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Crystal structure of the human caspase-1 C285A mutant after removal of malonate

X-ray diffraction
2.1Å resolution
PDB entry 1sc4 coloured by chain, front view.
PDB entry 1sc4 coloured by chain, side view.
PDB entry 1sc4 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-1 complex
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Multimeric state: hetero tetramer
Accessible surface area: 20441.41 Å2
Buried surface area: 14830.21 Å2
Dissociation area: 2,715.51 Å2
Dissociation energy (ΔGdiss): 22.22 kcal/mol
Dissociation entropy (TΔSdiss): 13.66 kcal/mol
Symmetry number: 2
PDBe Complex ID: PDB-CPX-151489
Complex Portal ID: CPX-952

Macromolecules

Caspase-1 subunit p20
Chain: A
Length: 178 amino acids
Theoretical weight: 19.84 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: P29466 (Residues: 120-297; Coverage: 44%)
Gene names: CASP1, IL1BC, IL1BCE
Pfam: Caspase domain
InterPro:
CATH: Rossmann fold
SCOP: Caspase catalytic domain
Caspase-1 subunit p20 in PDB entry 1sc4, assembly 1, front view.
Caspase-1 subunit p20 in PDB entry 1sc4, assembly 1, side view.
Caspase-1 subunit p20 in PDB entry 1sc4, assembly 1, top view.
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Caspase-1 subunit p10
Chain: B
Length: 88 amino acids
Theoretical weight: 10.26 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: P29466 (Residues: 317-404; Coverage: 22%)
Gene names: CASP1, IL1BC, IL1BCE
Pfam: Caspase domain
InterPro:
CATH: Caspase-like
SCOP: Caspase catalytic domain
Caspase-1 subunit p10 in PDB entry 1sc4, assembly 1, front view.
Caspase-1 subunit p10 in PDB entry 1sc4, assembly 1, side view.
Caspase-1 subunit p10 in PDB entry 1sc4, assembly 1, top view.
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