PDBe 3e4c

X-ray diffraction
2.05Å resolution

Procaspase-1 zymogen domain crystal strucutre

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:
homo dimer (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Caspase-1 subunit p20 Chains: A, B
Molecule details ›
Chains: A, B
Length: 302 amino acids
Theoretical weight: 33.8 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: P29466 (Residues: 104-404; Coverage: 75%)
Gene names: CASP1, IL1BC, IL1BCE
Sequence domains: Caspase domain
Structure domains: Rossmann fold

Ligands and Environments

1 bound ligand:

No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ALS BEAMLINE 5.0.1
Spacegroup: P1
Unit cell:
a: 56.1Å b: 58.004Å c: 60.12Å
α: 105.95° β: 119.6° γ: 92.77°
R-values:
R R work R free
0.204 0.2 0.263
Expression system: Escherichia coli