PDBe 2fqq

X-ray diffraction
3.3Å resolution

Crystal structure of human caspase-1 (Cys285->Ala, Cys362->Ala, Cys364->Ala, Cys397->Ala) in complex with 1-methyl-3-trifluoromethyl-1H-thieno[2,3-c]pyrazole-5-carboxylic acid (2-mercapto-ethyl)-amide

Released:
Source organism: Homo sapiens
Primary publication:
A common allosteric site and mechanism in caspases.
Proc. Natl. Acad. Sci. U.S.A. 103 7595-600 (2006)
PMID: 16682620

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: 10.16 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

1 bound ligand:

No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU RUH3R
Spacegroup: P3221
Unit cell:
a: 71.044Å b: 71.044Å c: 117.761Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.245 0.244 0.28
Expression system: Escherichia coli