PDBe 1sc4

X-ray diffraction
2.1Å resolution

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

Released:

Function and Biology Details

Reaction catalysed:
Strict requirement for an Asp residue at position P1 and has a preferred cleavage sequence of Tyr-Val-Ala-Asp-|-.
Biochemical function:
Biological process:
Cellular component:
  • not assigned

Structure analysis Details

Assembly composition:
hetero tetramer (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Caspase-1 subunit p20 Chain: A
Molecule details ›
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
Structure domains: Rossmann fold
Caspase-1 subunit p10 Chain: B
Molecule details ›
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
Structure domains: Caspase-like

Ligands and Environments

No bound ligands

No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU RUH3R
Spacegroup: P43212
Unit cell:
a: 62.982Å b: 62.982Å c: 143.158Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.223 0.221 0.258
Expression system: Escherichia coli