Targeting the PEX14-PEX5 interaction by small molecules provides novel therapeutic routes to treat trypanosomiases.

Structure

x-ray diffraction · 1 distinct chain · 73% helix, 0% strand (DSSP).

Ligands and binding sites

• KZZ · 1-(2-azanylethyl)-5-[(4-methoxynaphthalen-1-yl)methyl]-~{N}-(naphthalen-1-ylmethyl)-6,7-dihydro-4~{H}-pyrazolo[4,3-c]pyridine-3-carboxamide · ligand · 4 copies · chains A, B, D, F
• SO4 · Sulfate ion · ion · 6 copies · chains A, B, D
• CL · Chloride ion · ion · 2 copies · chains A, B
• BME · Beta-mercaptoethanol · additive · 4 copies · chains A, B, D, F

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

Pockets

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

Interfaces

3 interfaces between chains.

• A–B · 263 Ų buried · 3 hydrogen bonds · protein-protein
• A–F · 245 Ų buried · 4 hydrogen bonds · protein-protein
• B–D · 207 Ų buried · 3 hydrogen bonds · protein-protein

Compared structures

• 5N8V · Targeting the PEX14-PEX5 interaction by small molecules provides novel therapeutic routes… · the same entry in another collection · 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 Q8IEW2
• Elsewhere: RCSB PDB 5N8V · PDBe 5N8V · UniProt Q8IEW2