Journal:Acta Cryst D:S2059798322008373
From Proteopedia
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<b>Molecular Tour</b><br> | <b>Molecular Tour</b><br> | ||
| + | Crystal structure of bacterial nitroreductase (NR) NfsB in complex with the traditional medicine berberine (BBR) showed BBR binds into the active pocket at the NfsB dimer interface. BBR is mainly stabilized by π-stacking interactions with both neighboring aromatic residues and the cofactor FMN. Several well-ordered water molecules neighboring BBR in the active site probably donate protons in conjunction with electron transfer from FMN for BBR reduction. | ||
<b>References</b><br> | <b>References</b><br> | ||
Revision as of 11:16, 23 August 2022
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