This old version of Proteopedia is provided for student assignments while the new version is undergoing repairs. Content and edits done in this old version of Proteopedia after March 1, 2026 will eventually be lost when it is retired in about June of 2026.
Apply for new accounts at the new Proteopedia. Your logins will work in both the old and new versions.
User:Kirsten Reimer/Sandbox 1
From Proteopedia
< User:Kirsten Reimer(Difference between revisions)
| (13 intermediate revisions not shown.) | |||
| Line 1: | Line 1: | ||
| - | ==NADPH | + | ==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. | ||
| - | + | <scene name='58/580275/3es9/1'>cypor</scene> | |
| - | + | ||
| + | [[Image:Cypor.png]] | ||
</StructureSection> | </StructureSection> | ||
Current revision
NADPH Cytochrome P450 Oxidoreductase
| |||||||||||
