Flavin reductase
From Proteopedia
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<StructureSection load='1he2' size='350' side='right' scene='' caption='Human flavin reductase complex with biliverdin IX α and NADP (PDB code [[1he2]]) '> | <StructureSection load='1he2' size='350' side='right' scene='' caption='Human flavin reductase complex with biliverdin IX α and NADP (PDB code [[1he2]]) '> | ||
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FR catalytic reaction is the basis of the therapeutic use of methylene blue or riboflavin in the treatment of methemoglobinemia. Bacterial FR are used to sensitize tumors to drugs. | FR catalytic reaction is the basis of the therapeutic use of methylene blue or riboflavin in the treatment of methemoglobinemia. Bacterial FR are used to sensitize tumors to drugs. | ||
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| + | == Structural insights == | ||
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| + | The NADP containing active site can accommodate a variety of ligands because the binding is achieved via mainly hydrophobic interactions. | ||
</StructureSection> | </StructureSection> | ||
Revision as of 16:29, 22 January 2016
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3D structures of flavin reductase
Updated on 22-January-2016
1qfj – FR – Escherichia coli
1bkj – VhFR + FMN – Vibrio harveyi
2bkj - VhFR + NAD + FMN
1hdo - hFR + NADP - human
1he2 - hFR + biliverdin IX α + NADP
1he3 - hFR + mesobiliverdin IV α + NADP
1he4 - hFR + FMN + NADP
1he5 - hFR + lumichrome + NADP
1rz0 – GtFR + FAD – Geobacillus thermoglucosidasius
1rz1 - GtFR + FAD + NAD
3pft - FR (mutant) + FMN – Mycobacterium goodii
References
- ↑ Yubisui T, Takeshita M, Yoneyama Y. Reduction of methemoglobin through flavin at the physiological concentration by NADPH-flavin reductase of human erythrocytes. J Biochem. 1980 Jun;87(6):1715-20. PMID:7400118
