6saq: Difference between revisions

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'''Unreleased structure'''


The entry 6saq is ON HOLD  until Paper Publication
==wild-type NuoEF from Aquifex aeolicus bound to NADH-OH==
<StructureSection load='6saq' size='340' side='right'caption='[[6saq]], [[Resolution|resolution]] 2.02&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[6saq]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Aquifex_aeolicus_VF5 Aquifex aeolicus VF5]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6SAQ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6SAQ FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.02&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=FES:FE2/S2+(INORGANIC)+CLUSTER'>FES</scene>, <scene name='pdbligand=FMN:FLAVIN+MONONUCLEOTIDE'>FMN</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=L3W:[[(2~{R},3~{S},4~{R},5~{R})-5-(6-aminopurin-9-yl)-3,4-bis(oxidanyl)oxolan-2-yl]methoxy-oxidanyl-phosphoryl]+[(2~{R},3~{S},4~{R},5~{R})-5-[[(1~{E},3~{Z})-5-azanyl-4-oxidanyl-5-oxidanylidene-penta-1,3-dienyl]-methanoyl-amino]-3,4-bis(oxidanyl)oxolan-2-yl]methyl+hydrogen+phosphate'>L3W</scene></td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=6saq FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6saq OCA], [https://pdbe.org/6saq PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6saq RCSB], [https://www.ebi.ac.uk/pdbsum/6saq PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6saq ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/NUOE_AQUAE NUOE_AQUAE] NDH-1 shuttles electrons from NADH, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory chain. Couples the redox reaction to proton translocation (for every two electrons transferred, four hydrogen ions are translocated across the cytoplasmic membrane), and thus conserves the redox energy in a proton gradient (By similarity).


Authors: Gerhardt, S.
==See Also==
 
*[[NADH-quinone oxidoreductase|NADH-quinone oxidoreductase]]
Description: wild-type NuoEF from Aquifex aeolicus bound to NADH-OH
__TOC__
[[Category: Unreleased Structures]]
</StructureSection>
[[Category: Gerhardt, S]]
[[Category: Aquifex aeolicus VF5]]
[[Category: Large Structures]]
[[Category: Gerhardt S]]

Latest revision as of 18:36, 8 September 2026

wild-type NuoEF from Aquifex aeolicus bound to NADH-OH

6saq, resolution 2.02Å

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