User:Kirsten Reimer/Sandbox 1

==NADPH Cytochrome P450 Oxidoreductase==

==NADPH Cytochrome P450 Oxidoreductase==

<StructureSection load='3rec' size='340' side='right' caption='Caption for this structure' scene=''>

<StructureSection load='3rec' size='340' side='right' caption='Caption for this structure' scene=''>

'''[[NADPH Cytochrome P450 Oxidoreductase]]''' (or '''CYPOR''') is a part of the P450 Cytochrome family that functions in transferring electrons from NADPH via cofactors FAD and FMN to other P450 cytochromes in the endoplasmic reticulum. CYPOR is a multimeric enzyme approximately 78kDa in size. CYPOR contains an N-terminal α-helix that anchors it in the endoplasmic reticulum membrane. The most C-terminal domain acts to bind NADH and FAD, and the N-terminal domain before the transmembrane anchor binds FMN. The FMN and FAD binding domains are separated by a connecting domain, which plays a role in allowing conformational change during electron transfer between the two flavin-containing domains. Crystal structures indicate the FMN domain is mobile with respect to the other domains.

'''[[NADPH Cytochrome P450 Oxidoreductase]]''' (or '''CYPOR''') is a part of the P450 Cytochrome family that functions in transferring electrons from NADPH via cofactors FAD and FMN to other P450 cytochromes in the endoplasmic reticulum. CYPOR is a multimeric enzyme approximately 78kDa in size. CYPOR contains an N-terminal α-helix that anchors it in the endoplasmic reticulum membrane. The most C-terminal domain acts to bind NADH and FAD, and the N-terminal domain before the transmembrane anchor binds FMN. The FMN and FAD binding domains are separated by a connecting domain, which plays a role in allowing conformational change during electron transfer between the two flavin-containing domains. Crystal structures indicate the FMN domain is mobile with respect to the other domains.

</StructureSection>

</StructureSection>