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:
  • not assigned
Biological process:
  • not assigned
Cellular component:
  • not assigned

Structure analysis Details

Assembly composition:
hetero hexamer (preferred)
PDBe Complex ID:
PDB-CPX-151491 (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
TETRAPEPTIDE ALDEHYDE Chain: T
Molecule details ›
Chain: T
Length: 5 amino acids
Theoretical weight: 477 Da
Source organism: Synthetic construct
Expression system: Not provided
Caspase-1 subunit p10 Chain: B
Molecule details ›
Chain: B
Length: 88 amino acids
Theoretical weight: 10.26 KDa
Source organism: Homo sapiens

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
Expression system: Not provided