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7p64
From Proteopedia
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| - | '''Unreleased structure''' | ||
| - | + | ==Complex I from E. coli, DDM/LMNG-purified, under Turnover at pH 6, Open state== | |
| - | + | <StructureSection load='7p64' size='340' side='right'caption='[[7p64]], [[Resolution|resolution]] 2.50Å' scene=''> | |
| - | + | == Structural highlights == | |
| - | + | <table><tr><td colspan='2'>[[7p64]] is a 10 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli_BL21(DE3) Escherichia coli BL21(DE3)]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7P64 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7P64 FirstGlance]. <br> | |
| - | + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=3PE:1,2-DIACYL-SN-GLYCERO-3-PHOSPHOETHANOLAMINE'>3PE</scene>, <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=DCQ:2-DECYL-5,6-DIMETHOXY-3-METHYLCYCLOHEXA-2,5-DIENE-1,4-DIONE'>DCQ</scene>, <scene name='pdbligand=FES:FE2/S2+(INORGANIC)+CLUSTER'>FES</scene>, <scene name='pdbligand=FMN:FLAVIN+MONONUCLEOTIDE'>FMN</scene>, <scene name='pdbligand=LFA:EICOSANE'>LFA</scene>, <scene name='pdbligand=NAI:1,4-DIHYDRONICOTINAMIDE+ADENINE+DINUCLEOTIDE'>NAI</scene>, <scene name='pdbligand=SF4:IRON/SULFUR+CLUSTER'>SF4</scene></td></tr> | |
| - | [[Category: | + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=7p64 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7p64 OCA], [https://pdbe.org/7p64 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7p64 RCSB], [https://www.ebi.ac.uk/pdbsum/7p64 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7p64 ProSAT]</span></td></tr> |
| + | </table> | ||
| + | == Function == | ||
| + | [[https://www.uniprot.org/uniprot/A0A140N755_ECOBD A0A140N755_ECOBD]] NDH-1 shuttles electrons from NADH, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory chain. The immediate electron acceptor for the enzyme in this species is believed to be ubiquinone. 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.[HAMAP-Rule:MF_00445] | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Large Structures]] | ||
| + | [[Category: Kampjut D]] | ||
| + | [[Category: Kravchuk V]] | ||
| + | [[Category: Sazanov L]] | ||
Current revision
Complex I from E. coli, DDM/LMNG-purified, under Turnover at pH 6, Open state
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