PDBe 1ice

X-ray diffraction
2.6Å resolution

STRUCTURE AND MECHANISM OF INTERLEUKIN-1BETA CONVERTING ENZYME

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 hexamer (preferred)
Entry contents:
3 distinct polypeptide molecules
Macromolecules (3 distinct):
Caspase-1 subunit p20 Chain: A
Molecule details ›
Chain: A
Length: 167 amino acids
Theoretical weight: 18.81 KDa
Source organism: Homo sapiens
UniProt:
  • Canonical: P29466 (Residues: 131-297; Coverage: 41%)
Gene names: CASP1, IL1BC, IL1BCE
Structure domains: Rossmann fold
TETRAPEPTIDE ALDEHYDE Chain: T
Molecule details ›
Chain: T
Length: 5 amino acids
Theoretical weight: 477 Da
Caspase-1 subunit p10 Chain: B
Molecule details ›
Chain: B
Length: 88 amino acids
Theoretical weight: 10.26 KDa
Source organism: Homo sapiens
UniProt:
  • Canonical: P29466 (Residues: 317-404; Coverage: 22%)
Gene names: CASP1, IL1BC, IL1BCE
Structure domains: Caspase-like

Ligands and Environments

No bound ligands

1 modified residue:

Experiments and Validation Details

Entry percentile scores
Spacegroup: P43212
Unit cell:
a: 64.4Å b: 64.4Å c: 163.3Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.19 0.19 not available