Dear Harry,

You can check this structure of an FAD-dependent monooxygenase with bound FAD and NADPH: https://www.rcsb.org/structure/1k0j However, authors of this review (https://doi.org/10.3390/ijms131215601) seem not to be convinced about the NADPH position (if I remember that review right).

By the way, I would be interested in metal-metal interactions in biomolecules (if I can a bit hijack this thread...) I do not mean interactions like Mg-Cl-Mg, but clearly two metal atoms closer than ~3.6 A to each other.

Best wishes,
Martin


On 20/12/2024 11:07, Chandra Prakash Tiwari wrote:
Yes, multiple cofactors can exist in active sites. One example is Enolase. Also, metal-metal bonds are common in coordination spheres for catalysis.

On Fri, Dec 20, 2024 at 4:34 PM David Briggs <david.bri...@crick.ac.uk> wrote:

    Hi Harry,

    The first thing that comes to mind is any sort of light harvesting
    complex - take a look at 1RWT. Would that fit the bill?

    D



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    molecules...were just as experiments suggested?"

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    *From:* CCP4 bulletin board <CCP4BB@JISCMAIL.AC.UK> on behalf of
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    *Sent:* 20 December 2024 10:37
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    *Subject:* [ccp4bb] enzyme or other protein with multiple cofactors

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    Hi folks

    I’m familiar with enzymes that have a single co-factor (for
    example haem in myoglobin [or in the individual chains in
    haemoglobins] or FAD in flavoproteins), but was wondering if there
    are examples of single-chain proteins that have multiple cofactors
    (or even multiple chain proteins that have multiple cofactors
    bound to a single chain)?

    I’m not bothered (at the moment) about proteins that have
    cofactors bound to different chains.

    I thought this would be a good place to ask…

    Harry
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