Development of N-(functionalized benzoyl)-homocycloleucyl- glycinonitriles as potent cathepsin K inhibitors.

Structure

x-ray diffraction · 1 distinct chain · 28% helix, 23% strand (DSSP).

Ligands and binding sites

• 3Y2 · 2-amino-4-chloro-N-(1-{[(2E)-2-iminoethyl]carbamoyl}cyclohexyl)benzamide · ligand · chains A
• K · Potassium ion · metal · chains A
• CL · Chloride ion · ion · chains A
• PGO · S-1,2-propanediol · additive · 3 copies · chains A
• GOL · Glycerol · additive · chains A

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

Pockets

1 pocket found on a 1 Å grid, 0 with a druggability of 0.5 or more.

Modifications

Observed in the structure: 3 disulfide, 1 covalent (disulfide, covalent ligand).

Compared structures

• 4X6J · Development of N-(Functionalized benzoyl)-homocycloleucyl-glycinonitriles as Potent… · the same entry in another collection · chain A against A, TM-score 1.00
• P43235 · AlphaFold monomer V2.0 prediction for cathepsin K (P43235) · a predicted model of the same protein · chain A against A, TM-score 1.00

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 P43235
• Elsewhere: RCSB PDB 4X6J · PDBe 4X6J · UniProt P43235