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3hb3

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Current revision (07:19, 6 September 2023) (edit) (undo)
 
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<StructureSection load='3hb3' size='340' side='right'caption='[[3hb3]], [[Resolution|resolution]] 2.25&Aring;' scene=''>
<StructureSection load='3hb3' size='340' side='right'caption='[[3hb3]], [[Resolution|resolution]] 2.25&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[3hb3]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Atcc_17741 Atcc 17741] and [https://en.wikipedia.org/wiki/Lk3_transgenic_mice Lk3 transgenic mice]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3HB3 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3HB3 FirstGlance]. <br>
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<table><tr><td colspan='2'>[[3hb3]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Mus_musculus Mus musculus] and [https://en.wikipedia.org/wiki/Paracoccus_denitrificans Paracoccus denitrificans]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3HB3 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3HB3 FirstGlance]. <br>
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</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=LDA:LAURYL+DIMETHYLAMINE-N-OXIDE'>LDA</scene>, <scene name='pdbligand=LMT:DODECYL-BETA-D-MALTOSIDE'>LMT</scene>, <scene name='pdbligand=MN:MANGANESE+(II)+ION'>MN</scene>, <scene name='pdbligand=PEO:HYDROGEN+PEROXIDE'>PEO</scene></td></tr>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.25&#8491;</td></tr>
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<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[1ar1|1ar1]]</div></td></tr>
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<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=LDA:LAURYL+DIMETHYLAMINE-N-OXIDE'>LDA</scene>, <scene name='pdbligand=LMT:DODECYL-BETA-D-MALTOSIDE'>LMT</scene>, <scene name='pdbligand=MN:MANGANESE+(II)+ION'>MN</scene>, <scene name='pdbligand=PEO:HYDROGEN+PEROXIDE'>PEO</scene></td></tr>
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<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">ctaDII ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=266 ATCC 17741]), ctaC, coiI, ctaB ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=266 ATCC 17741])</td></tr>
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<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>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=3hb3 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3hb3 OCA], [https://pdbe.org/3hb3 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3hb3 RCSB], [https://www.ebi.ac.uk/pdbsum/3hb3 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3hb3 ProSAT]</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=3hb3 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3hb3 OCA], [https://pdbe.org/3hb3 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3hb3 RCSB], [https://www.ebi.ac.uk/pdbsum/3hb3 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3hb3 ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
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[[https://www.uniprot.org/uniprot/COX1B_PARDE COX1B_PARDE]] Subunit 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). This cytochrome c oxidase shows proton pump activity across the membrane in addition to the electron transfer. [[https://www.uniprot.org/uniprot/COX2_PARDE COX2_PARDE]] 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).
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[https://www.uniprot.org/uniprot/HVM54_MOUSE HVM54_MOUSE]
== Evolutionary Conservation ==
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
[[Image:Consurf_key_small.gif|200px|right]]
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__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: Atcc 17741]]
 
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[[Category: Cytochrome-c oxidase]]
 
[[Category: Large Structures]]
[[Category: Large Structures]]
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[[Category: Lk3 transgenic mice]]
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[[Category: Mus musculus]]
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[[Category: Angerer, H]]
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[[Category: Paracoccus denitrificans]]
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[[Category: Koepke, J]]
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[[Category: Angerer H]]
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[[Category: Peng, G]]
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[[Category: Koepke J]]
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[[Category: Cell inner membrane]]
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[[Category: Peng G]]
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[[Category: Cell membrane]]
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[[Category: Copper]]
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[[Category: Disulfide bond]]
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[[Category: Electron transfer]]
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[[Category: Electron transport]]
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[[Category: Heme]]
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[[Category: Hydrogen ion transport]]
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[[Category: Ion transport]]
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[[Category: Iron]]
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[[Category: Membrane]]
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[[Category: Membrane protein]]
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[[Category: Metal-binding]]
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[[Category: Oxidoreductase]]
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[[Category: Proton pumping]]
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[[Category: Proton transfer]]
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[[Category: Pyrrolidone carboxylic acid]]
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[[Category: Respiratory chain]]
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[[Category: Transmembrane]]
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[[Category: Transport]]
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Current revision

High resolution crystal structure of Paracoccus denitrificans cytochrome c oxidase

PDB ID 3hb3

Drag the structure with the mouse to rotate

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