Synthesis of casimiroin and optimization of its quinone reductase 2 and aromatase inhibitory activity

Structure

x-ray diffraction · 1 distinct chain · 40% helix, 16% strand (DSSP).

Ligands and binding sites

• XM5 · 6-methoxy-9-methyl[1,3]dioxolo[4,5-h]quinolin-8(9H)-one · ligand · 4 copies · chains A, B
• FAD · Flavin-adenine dinucleotide · ligand · 2 copies · chains A, B
• ZN · Zinc ion · metal · 2 copies · chains A, B

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

Pockets

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

Interfaces

1 interface between chains.

• A–B · 2041 Ų buried · 26 hydrogen bonds · protein-protein

Compared structures

• 3G5M · Synthesis of Casimiroin and Optimization of Its Qui Reductase 2 and Aromatase Inhibitory… · the same entry in another collection · chain A against A, TM-score 1.00
• P16083 · AlphaFold monomer V2.0 prediction for ribosyldihydronicotinamide dehydrogenase [quinone]… · 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 P16083
• Elsewhere: RCSB PDB 3G5M · PDBe 3G5M · UniProt P16083