3vr9: Difference between revisions

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'''Unreleased structure'''
{{STRUCTURE_3vr9|  PDB=3vr9  |  SCENE=  }}
===Mitochondrial rhodoquinol-fumarate reductase from the parasitic nematode Ascaris suum with the specific inhibitor flutolanil===


The entry 3vr9 is ON HOLD  until Paper Publication
==Function==
[[http://www.uniprot.org/uniprot/DHSD_ASCSU DHSD_ASCSU]] Membrane-anchoring subunit of succinate dehydrogenase (SDH) that is involved in complex II of the mitochondrial electron transport chain and is responsible for transferring electrons from succinate to ubiquinone (coenzyme Q) (By similarity).


Authors: Shimizu, H., Shiba, T., Inaoka, D.K., Osanai, A., Kita, K., Sakamoto, K., Harada, S.
==About this Structure==
 
[[3vr9]] is a 8 chain structure with sequence from [http://en.wikipedia.org/wiki/Ascaris_suum Ascaris suum]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3VR9 OCA].  
Description: Mitochondrial rhodoquinol-fumarate reductase from the parasitic nematode Ascaris suum with the specific inhibitor flutolanil
[[Category: Ascaris suum]]
[[Category: Harada, S.]]
[[Category: Inaoka, D K.]]
[[Category: Kita, K.]]
[[Category: Osanai, A.]]
[[Category: Sakamoto, K.]]
[[Category: Shiba, T.]]
[[Category: Shimizu, H.]]
[[Category: Ascaris suum]]
[[Category: Membrane protein]]
[[Category: Mitochondrial membrane]]
[[Category: Oxidoreductase-oxidoreductase inhibitor complex]]
[[Category: Reductase]]

Revision as of 22:37, 10 April 2013

Template:STRUCTURE 3vr9

Mitochondrial rhodoquinol-fumarate reductase from the parasitic nematode Ascaris suum with the specific inhibitor flutolanil

Function

[DHSD_ASCSU] Membrane-anchoring subunit of succinate dehydrogenase (SDH) that is involved in complex II of the mitochondrial electron transport chain and is responsible for transferring electrons from succinate to ubiquinone (coenzyme Q) (By similarity).

About this Structure

3vr9 is a 8 chain structure with sequence from Ascaris suum. Full crystallographic information is available from OCA.

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