5b3p
From Proteopedia
(Difference between revisions)
| (3 intermediate revisions not shown.) | |||
| Line 1: | Line 1: | ||
| - | '''Unreleased structure''' | ||
| - | + | ==Nqo5 of the trypsin-resistant fragment (1-134) in P212121 form== | |
| + | <StructureSection load='5b3p' size='340' side='right'caption='[[5b3p]], [[Resolution|resolution]] 1.65Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[5b3p]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Thermus_thermophilus_HB8 Thermus thermophilus HB8]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5B3P OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5B3P 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]] 1.652Å</td></tr> | ||
| + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</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=5b3p FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5b3p OCA], [https://pdbe.org/5b3p PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5b3p RCSB], [https://www.ebi.ac.uk/pdbsum/5b3p PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5b3p ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | == Function == | ||
| + | [https://www.uniprot.org/uniprot/NQO5_THET8 NQO5_THET8] 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 menaquinone. 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 required for the synthesis of ATP. The nqo5 subunit may be involved in the stabilization of the complex.[HAMAP-Rule:MF_01357] | ||
| - | + | ==See Also== | |
| - | + | *[[NADH-quinone oxidoreductase|NADH-quinone oxidoreductase]] | |
| - | + | __TOC__ | |
| - | [[Category: | + | </StructureSection> |
| + | [[Category: Large Structures]] | ||
| + | [[Category: Thermus thermophilus HB8]] | ||
| + | [[Category: Hanazono Y]] | ||
| + | [[Category: Miki K]] | ||
| + | [[Category: Takeda K]] | ||
Current revision
Nqo5 of the trypsin-resistant fragment (1-134) in P212121 form
| |||||||||||
