5weh: Difference between revisions

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 <StructureSection load='5weh' size='340' side='right'caption='[[5weh]], [[Resolution|resolution]] 3.45&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[5weh]] is a 8 chain structure with sequence from [https://en.wikipedia.org/wiki/"luteovulum_sphaeroides"_(van_niel_1944)_suresh_et_al._2019 "luteovulum sphaeroides" (van niel 1944) suresh et al. 2019]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5WEH OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5WEH FirstGlance]. <br>
+<table><tr><td colspan='2'>[[5weh]] is a 8 chain structure with sequence from [https://en.wikipedia.org/wiki/Cereibacter_sphaeroides Cereibacter sphaeroides]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5WEH OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5WEH FirstGlance]. <br>
-</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>, <scene name='pdbligand=CU1:COPPER+(I)+ION'>CU1</scene>, <scene name='pdbligand=HEA:HEME-A'>HEA</scene>, <scene name='pdbligand=LMU:DODECYL-ALPHA-D-MALTOSIDE'>LMU</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=PEH:DI-STEAROYL-3-SN-PHOSPHATIDYLETHANOLAMINE'>PEH</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]] 3.45&#8491;</td></tr>
-<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">ctaD ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1063 "Luteovulum sphaeroides" (van Niel 1944) Suresh et al. 2019]), ctaC, coxII, ctaB ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1063 "Luteovulum sphaeroides" (van Niel 1944) Suresh et al. 2019]), coxIV ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1063 "Luteovulum sphaeroides" (van Niel 1944) Suresh et al. 2019])</td></tr>
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=3PE:1,2-DIACYL-SN-GLYCERO-3-PHOSPHOETHANOLAMINE'>3PE</scene>, <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=CU1:COPPER+(I)+ION'>CU1</scene>, <scene name='pdbligand=HEA:HEME-A'>HEA</scene>, <scene name='pdbligand=LMU:DODECYL-ALPHA-D-MALTOSIDE'>LMU</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene></td></tr>
-<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/Cytochrome-c_oxidase Cytochrome-c oxidase], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.9.3.1 1.9.3.1] </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=5weh FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5weh OCA], [https://pdbe.org/5weh PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5weh RCSB], [https://www.ebi.ac.uk/pdbsum/5weh PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5weh ProSAT]</span></td></tr>
 </table>
 == Function ==
-[[https://www.uniprot.org/uniprot/COX1_RHOSH COX1_RHOSH]] Cytochrome c oxidase is the component of the respiratory chain that catalyzes the reduction of oxygen to water. Subunits 1-3 form the functional core of the enzyme complex. Co I is the catalytic subunit of the enzyme. Electrons originating in cytochrome c are transferred via the copper A center of subunit 2 and heme a of subunit 1 to the bimetallic center formed by heme a3 and copper B. This cytochrome c oxidase shows proton pump activity across the membrane in addition to the electron transfer. [[https://www.uniprot.org/uniprot/COX2_RHOSH COX2_RHOSH]] Subunits I and II form the functional core of the enzyme complex. Electrons originating in cytochrome c are transferred via heme a and Cu(A) to the binuclear center formed by heme a3 and Cu(B).
+[https://www.uniprot.org/uniprot/COX1_CERSP COX1_CERSP] Cytochrome c oxidase is the component of the respiratory chain that catalyzes the reduction of oxygen to water. Subunits 1-3 form the functional core of the enzyme complex. Co I is the catalytic subunit of the enzyme. Electrons originating in cytochrome c are transferred via the copper A center of subunit 2 and heme a of subunit 1 to the bimetallic center formed by heme a3 and copper B. This cytochrome c oxidase shows proton pump activity across the membrane in addition to the electron transfer.
 <div style="background-color:#fffaf0;">
 == Publication Abstract from PubMed ==
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 __TOC__
 </StructureSection>
-[[Category: Cytochrome-c oxidase]]
+[[Category: Cereibacter sphaeroides]]
 [[Category: Large Structures]]
-[[Category: Ferguson-Miller, F]]
+[[Category: Ferguson-Miller F]]
-[[Category: Hiser, C]]
+[[Category: Hiser C]]
-[[Category: Ling, Q]]
+[[Category: Ling Q]]
-[[Category: Liu, J]]
+[[Category: Liu J]]
-[[Category: Complex iv]]
-[[Category: Oxidase]]
-[[Category: Oxidoreductase]]
-[[Category: Reduced]]