The structure of cathepsin S with a novel 2- arylphenoxyacetaldehyde inhibitor derived by the substrate activity screening (sas) method

Structure

x-ray diffraction · 1 distinct chain · 29% helix, 24% strand (DSSP).

Ligands and binding sites

• TF5 · 2-[(2',3',4'-trifluorobiphenyl-2-yl)oxy]ethanol · ligand · 2 copies · chains A, B
• PEU · 2,5,8,11,14,17,20,23,26,29,32,35,38,41,44,47,50,53,56, 59,62,65,68,71,74,77,80-heptacosaoxadooctacontan-82-ol · ligand · chains A, B
• SO4 · Sulfate ion · ion · chains A

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 · 764 Ų buried · 6 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 6 disulfide, 2 covalent (disulfide, covalent ligand).

Compared structures

• 2OP3 · The structure of cathepsin S with a novel 2-arylphenoxyacetaldehyde inhibitor derived by… · the same entry in another collection · chain A against A, TM-score 1.00
• P25774 · AlphaFold monomer V2.0 prediction for cathepsin S (P25774) · 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 P25774
• Elsewhere: RCSB PDB 2OP3 · PDBe 2OP3 · UniProt P25774