Crystal structure of human caspase-1 with 2-((2-naphthoyl)-L-valyl)-4- hydroxy-N-((3S)-2-hydroxy-5-oxotetrahydrofuran-3-yl)-2- AZABICYCLO[2.2.2]OCTANE-3-carboxamide (compound 1)

Structure

x-ray diffraction · 2 distinct chains · 29% helix, 19% strand (DSSP).

Ligands and binding sites

• WE0 · (3~{S})-3-[[(3~{S})-2-[(2~{S})-3-methyl-2-(naphthalen-2-ylcarbonylamino)butanoyl]-4-oxidanyl-2-azabicyclo[2.2.2]octan-3-yl]carbonylamino]-4-oxidanyl-butanoic acid · ligand · chains A, B

Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.

Pockets

2 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.

Interfaces

1 interface between chains.

• A–B · 2690 Ų buried · 51 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 1 covalent (covalent ligand).

Compared structures

• 5MMV · Crystal structure of human Caspase-1 with 2-((2-naphthoyl)-L-valyl)-4-hydroxy-N-((3S)-2-hy… · the same entry in another collection · chain A against A, TM-score 1.00
• P29466 · AlphaFold monomer V2.0 prediction for caspase-1 (P29466) · a predicted model of the same protein · chain B against A, TM-score 0.97

Analyse

• Open in the research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides and crosslinks on the 3D structure
• Every structure of UniProt P29466
• Elsewhere: RCSB PDB 5MMV · PDBe 5MMV · UniProt P29466