5dn6: Difference between revisions

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 ==ATP synthase from Paracoccus denitrificans==
-<StructureSection load='5dn6' size='340' side='right' caption='[[5dn6]], [[Resolution|resolution]] 3.98&Aring;' scene=''>
+<StructureSection load='5dn6' size='340' side='right'caption='[[5dn6]], [[Resolution|resolution]] 3.98&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[5dn6]] is a 29 chain structure with sequence from [http://en.wikipedia.org/wiki/Paracoccus_denitrificans Paracoccus denitrificans]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5DN6 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5DN6 FirstGlance]. <br>
+<table><tr><td colspan='2'>[[5dn6]] is a 25 chain structure with sequence from [https://en.wikipedia.org/wiki/Paracoccus_denitrificans Paracoccus denitrificans]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5DN6 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5DN6 FirstGlance]. <br>
-</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><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>
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 3.98&#8491;</td></tr>
-<tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=UNK:UNKNOWN'>UNK</scene></td></tr>
+<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>
-<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[5cdf|5cdf]], [[2xnd|2xnd]], [[2xok|2xok]]</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=5dn6 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5dn6 OCA], [https://pdbe.org/5dn6 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5dn6 RCSB], [https://www.ebi.ac.uk/pdbsum/5dn6 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5dn6 ProSAT]</span></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='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=5dn6 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5dn6 OCA], [http://pdbe.org/5dn6 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5dn6 RCSB], [http://www.ebi.ac.uk/pdbsum/5dn6 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5dn6 ProSAT]</span></td></tr>
 </table>
 == Function ==
-[[http://www.uniprot.org/uniprot/ATPG_PARDP ATPG_PARDP]] Produces ATP from ADP in the presence of a proton gradient across the membrane. The gamma chain is believed to be important in regulating ATPase activity and the flow of protons through the CF(0) complex. [[http://www.uniprot.org/uniprot/ATPD_PARDP ATPD_PARDP]] 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.[HAMAP-Rule:MF_01416]  This protein is part of the stalk that links CF(0) to CF(1). It either transmits conformational changes from CF(0) to CF(1) or is implicated in proton conduction.[HAMAP-Rule:MF_01416] [[http://www.uniprot.org/uniprot/ATPE_PARDP ATPE_PARDP]] Produces ATP from ADP in the presence of a proton gradient across the membrane. [[http://www.uniprot.org/uniprot/ATPA_PARDP ATPA_PARDP]] Produces ATP from ADP in the presence of a proton gradient across the membrane. The alpha chain is a regulatory subunit. [[http://www.uniprot.org/uniprot/ATPB_PARDP ATPB_PARDP]] Produces ATP from ADP in the presence of a proton gradient across the membrane. The catalytic sites are hosted primarily by the beta subunits.
+[https://www.uniprot.org/uniprot/ATPA_PARDP ATPA_PARDP] Produces ATP from ADP in the presence of a proton gradient across the membrane. The alpha chain is a regulatory subunit.
 <div style="background-color:#fffaf0;">
 == Publication Abstract from PubMed ==
@@ Line 23: / Line 21: @@
 ==See Also==
-*[[ATPase|ATPase]]
+*[[ATPase 3D structures|ATPase 3D structures]]
 == References ==
 <references/>
 __TOC__
 </StructureSection>
+[[Category: Large Structures]]
 [[Category: Paracoccus denitrificans]]
-[[Category: Leslie, A G.W]]
+[[Category: Leslie AGW]]
-[[Category: Montgomery, M G]]
+[[Category: Montgomery MG]]
-[[Category: Morales-Rios, E]]
+[[Category: Morales-Rios E]]
-[[Category: Walker, J E]]
+[[Category: Walker JE]]
-[[Category: Atp synthase]]
-[[Category: Complex]]
-[[Category: Hydrolase]]
-[[Category: Paracoccus denitrifican]]
-[[Category: Proton translocation]]
-[[Category: Regulation]]