1b9u: Difference between revisions

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 ==MEMBRANE DOMAIN OF THE SUBUNIT B OF THE E.COLI ATP SYNTHASE==
-<StructureSection load='1b9u' size='340' side='right' caption='[[1b9u]], [[NMR_Ensembles_of_Models | 10 NMR models]]' scene=''>
+<StructureSection load='1b9u' size='340' side='right'caption='[[1b9u]]' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[1b9u]] is a 1 chain structure. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1B9U OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1B9U FirstGlance]. <br>
+<table><tr><td colspan='2'>[[1b9u]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli_K-12 Escherichia coli K-12]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1B9U OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1B9U FirstGlance]. <br>
-</td></tr><tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=GMA:4-AMIDO-4-CARBAMOYL-BUTYRIC+ACID'>GMA</scene></td></tr>
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR</td></tr>
-<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/H(+)-transporting_two-sector_ATPase H(+)-transporting two-sector ATPase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.6.3.14 3.6.3.14] </span></td></tr>
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GMA:4-AMIDO-4-CARBAMOYL-BUTYRIC+ACID'>GMA</scene></td></tr>
-<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1b9u FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1b9u OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1b9u RCSB], [http://www.ebi.ac.uk/pdbsum/1b9u PDBsum]</span></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=1b9u FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1b9u OCA], [https://pdbe.org/1b9u PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1b9u RCSB], [https://www.ebi.ac.uk/pdbsum/1b9u PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1b9u ProSAT]</span></td></tr>
 </table>
+== Function ==
+[https://www.uniprot.org/uniprot/ATPF_ECOLI ATPF_ECOLI] F(1)F(0) ATP synthase produces ATP from ADP in the presence of a proton or sodium gradient. 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 (By similarity).<ref>PMID:1682301</ref>   Component of the F(0) channel, it forms part of the peripheral stalk, linking F(1) to F(0) (By similarity).<ref>PMID:1682301</ref>
 == Evolutionary Conservation ==
 [[Image:Consurf_key_small.gif|200px|right]]
 Check<jmol>
    <jmolCheckbox>
-     <scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/b9/1b9u_consurf.spt"</scriptWhenChecked>
+     <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/b9/1b9u_consurf.spt"</scriptWhenChecked>
      <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
      <text>to colour the structure by Evolutionary Conservation</text>
    </jmolCheckbox>
-</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/chain_selection.php?pdb_ID=2ata ConSurf].
+</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1b9u ConSurf].
 <div style="clear:both"></div>
 <div style="background-color:#fffaf0;">
@@ Line 25: / Line 28: @@
 From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
 </div>
+<div class="pdbe-citations 1b9u" style="background-color:#fffaf0;"></div>
 ==See Also==
-*[[ATPase|ATPase]]
+*[[ATPase 3D structures|ATPase 3D structures]]
 == References ==
 <references/>
 __TOC__
 </StructureSection>
-[[Category: Dmitriev, O]]
+[[Category: Escherichia coli K-12]]
-[[Category: Fillingame, R H]]
+[[Category: Large Structures]]
-[[Category: Jiang, W]]
+[[Category: Dmitriev O]]
-[[Category: Jones, P C]]
+[[Category: Fillingame RH]]
-[[Category: Atp synthase]]
+[[Category: Jiang W]]
-[[Category: Hydrolase]]
+[[Category: Jones PC]]
-[[Category: Membrane protein]]