Flavin reductase

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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]]) '>
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<StructureSection load='1he2' size='450' side='right' scene='49/490853/Cv/1' caption='Human flavin reductase complex with biliverdin IX α and NADP (PDB code [[1he2]]) '>
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== Function ==
== Function ==
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== Structural insights ==
== Structural insights ==
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The NADP containing active site can accommodate a variety of ligands because the binding is achieved mainly via hydrophobic interactions<ref>PMID:11224564</ref>.
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The <scene name='49/490853/Cv/3'>NADP containing active site can accommodate a variety of ligands</scene> because the binding is achieved mainly via hydrophobic interactions ({{Template:ColorKey_Hydrophobic}}, {{Template:ColorKey_Polar}}).<ref>PMID:11224564</ref>
</StructureSection>
</StructureSection>

Revision as of 11:16, 26 January 2016

Human flavin reductase complex with biliverdin IX α and NADP (PDB code 1he2)

Drag the structure with the mouse to rotate

3D structures of flavin reductase

Updated on 26-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

  1. ↑ 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
  2. ↑ Pereira PJ, Macedo-Ribeiro S, Parraga A, Perez-Luque R, Cunningham O, Darcy K, Mantle TJ, Coll M. Structure of human biliverdin IXbeta reductase, an early fetal bilirubin IXbeta producing enzyme. Nat Struct Biol. 2001 Mar;8(3):215-20. PMID:11224564 doi:10.1038/84948

Proteopedia Page Contributors and Editors (what is this?)

Michal Harel, Alexander Berchansky, Joel L. Sussman

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