Crystal structure of human kinesin EG5 in complex with (R)- MON97, a new monastrol-based inhibitor that binds as (R)- enantiomer

Structure

x-ray diffraction · 2 distinct chains · 31% helix, 31% strand (DSSP).

Ligands and binding sites

• ADP · Adenosine-5'-diphosphate · ligand · 2 copies · chains A, B
• MOY · [(4R)-4-(3-hydroxyphenyl)-1,6-dimethyl-2-thioxo-1,2,3,4-tetrahydropyrimidin-5-yl](phenyl)methanone · ligand · 2 copies · chains A, B
• MG · Magnesium ion · metal · 2 copies · chains A, B
• K · Potassium ion · metal · chains A
• CL · Chloride ion · ion · chains A
• PG4 · Tetraethylene glycol · additive · chains A

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

Pockets

8 pockets found on a 1 Å grid, 5 with a druggability of 0.5 or more.

Interfaces

1 interface between chains.

• A–B · 205 Ų buried · 3 hydrogen bonds · protein-protein

Compared structures

• 2IEH · Crystal structure of human kinesin Eg5 in complex with (R)-mon97, a new monastrol-based… · 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 P52732
• Elsewhere: RCSB PDB 2IEH · PDBe 2IEH · UniProt P52732