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

Structure

x-ray diffraction · 1 distinct chain · 74% helix, 0% strand (DSSP).

Ligands and binding sites

• 6RB · 1-(2-hydroxyethyl)-5-[(4-methoxynaphthalen-1-yl) methyl]-~{N}-(phenylmethyl)-6,7-dihydro-4~{H}-pyrazolo[4,3-c]pyridine-3-carboxamide · ligand · 4 copies · chains A, B, C, D
• GLY · Glycine · ligand · chains A, C
• NA · Sodium ion · metal · chains C
• EDO · 1,2-ethanediol · additive · chains A, D

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

Pockets

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

Interfaces

4 interfaces between chains.

• A–B · 301 Ų buried · 2 hydrogen bonds · protein-protein
• A–D · 259 Ų buried · 2 hydrogen bonds · protein-protein
• B–C · 224 Ų buried · 0 hydrogen bonds · protein-protein
• A–C · 140 Ų buried · 0 hydrogen bonds · protein-protein

Compared structures

• 5L8A · 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 5L8A · PDBe 5L8A · UniProt Q8IEW2