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8h9v
From Proteopedia
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| - | '''Unreleased structure''' | ||
| - | + | ==Human ATP synthase state 3b (combined)== | |
| - | + | <StructureSection load='8h9v' size='340' side='right'caption='[[8h9v]], [[Resolution|resolution]] 3.02Å' scene=''> | |
| - | + | == Structural highlights == | |
| - | + | <table><tr><td colspan='2'>[[8h9v]] is a 17 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=8H9V OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=8H9V FirstGlance]. <br> | |
| - | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Electron Microscopy, [[Resolution|Resolution]] 3.02Å</td></tr> | |
| - | [[Category: | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ADP:ADENOSINE-5-DIPHOSPHATE'>ADP</scene>, <scene name='pdbligand=ATP:ADENOSINE-5-TRIPHOSPHATE'>ATP</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</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=8h9v FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=8h9v OCA], [https://pdbe.org/8h9v PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=8h9v RCSB], [https://www.ebi.ac.uk/pdbsum/8h9v PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=8h9v ProSAT]</span></td></tr> |
| - | [[Category: Gao | + | </table> |
| - | [[Category: | + | == Function == |
| - | [[Category: Lai | + | [https://www.uniprot.org/uniprot/AT5G1_HUMAN AT5G1_HUMAN] Mitochondrial membrane ATP synthase (F(1)F(0) ATP synthase or Complex V) produces ATP from ADP in the presence of a proton gradient across the membrane which is generated by electron transport complexes of the respiratory chain. F-type ATPases consist of two structural domains, F(1) - containing the extramembraneous catalytic core and F(0) - containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation. Part of the complex F(0) domain. A homomeric c-ring of probably 10 subunits is part of the complex rotary element. |
| - | [[Category: | + | __TOC__ |
| - | [[Category: | + | </StructureSection> |
| + | [[Category: Homo sapiens]] | ||
| + | [[Category: Large Structures]] | ||
| + | [[Category: Gao Y]] | ||
| + | [[Category: Gong H]] | ||
| + | [[Category: Lai Y]] | ||
| + | [[Category: Liu F]] | ||
| + | [[Category: Rao Z]] | ||
| + | [[Category: Zhang Y]] | ||
Current revision
Human ATP synthase state 3b (combined)
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Categories: Homo sapiens | Large Structures | Gao Y | Gong H | Lai Y | Liu F | Rao Z | Zhang Y
