8h9m: Difference between revisions
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== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[8h9m]] 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=8H9M OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=8H9M FirstGlance]. <br> | <table><tr><td colspan='2'>[[8h9m]] 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=8H9M OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=8H9M FirstGlance]. <br> | ||
</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=8h9m FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=8h9m OCA], [https://pdbe.org/8h9m PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=8h9m RCSB], [https://www.ebi.ac.uk/pdbsum/8h9m PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=8h9m ProSAT]</span></td></tr> | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Electron Microscopy, [[Resolution|Resolution]] 3Å</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=8h9m FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=8h9m OCA], [https://pdbe.org/8h9m PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=8h9m RCSB], [https://www.ebi.ac.uk/pdbsum/8h9m PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=8h9m ProSAT]</span></td></tr> | |||
</table> | </table> | ||
== Function == | == Function == | ||
Revision as of 08:55, 5 July 2023
Human ATP synthase state 3a subregion 3Human ATP synthase state 3a subregion 3
Structural highlights
FunctionAT5G1_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. |
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