2c1d: Difference between revisions

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<StructureSection load='2c1d' size='340' side='right'caption='[[2c1d]], [[Resolution|resolution]] 1.92&Aring;' scene=''>
<StructureSection load='2c1d' size='340' side='right'caption='[[2c1d]], [[Resolution|resolution]] 1.92&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[2c1d]] is a 8 chain structure with sequence from [https://en.wikipedia.org/wiki/Atcc_17741 Atcc 17741] and [https://en.wikipedia.org/wiki/Atcc_35512 Atcc 35512]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2C1D OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2C1D FirstGlance]. <br>
<table><tr><td colspan='2'>[[2c1d]] is a 8 chain structure with sequence from [https://en.wikipedia.org/wiki/Paracoccus_denitrificans Paracoccus denitrificans] and [https://en.wikipedia.org/wiki/Paracoccus_pantotrophus Paracoccus pantotrophus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2C1D OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2C1D FirstGlance]. <br>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=HEC:HEME+C'>HEC</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</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]] 1.92&#8491;</td></tr>
<tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=CSS:S-MERCAPTOCYSTEINE'>CSS</scene></td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CSS:S-MERCAPTOCYSTEINE'>CSS</scene>, <scene name='pdbligand=HEC:HEME+C'>HEC</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></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=2c1d FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2c1d OCA], [https://pdbe.org/2c1d PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2c1d RCSB], [https://www.ebi.ac.uk/pdbsum/2c1d PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2c1d 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=2c1d FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2c1d OCA], [https://pdbe.org/2c1d PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2c1d RCSB], [https://www.ebi.ac.uk/pdbsum/2c1d PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2c1d ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
[[https://www.uniprot.org/uniprot/SOXA_PARPN SOXA_PARPN]] C-type diheme cytochrome, which is part of the SoxAX cytochrome complex involved in sulfur oxidation. The SoxAX complex catalyzes the formation of a heterodisulfide bond between the conserved cysteine residue on a sulfur carrier SoxYZ complex subunit SoxY and thiosulfate or other inorganic sulfur substrates. This leads to the liberation of two electrons, which may be transferred from the SoxAX complex to another cytochrome c that then channels them into the respiratory electron transport chain. Some electrons may be used for reductive CO(2) fixation.<ref>PMID:10940005</ref> <ref>PMID:16297640</ref> <ref>PMID:17547421</ref>
[https://www.uniprot.org/uniprot/SOXA_PARPN SOXA_PARPN] C-type diheme cytochrome, which is part of the SoxAX cytochrome complex involved in sulfur oxidation. The SoxAX complex catalyzes the formation of a heterodisulfide bond between the conserved cysteine residue on a sulfur carrier SoxYZ complex subunit SoxY and thiosulfate or other inorganic sulfur substrates. This leads to the liberation of two electrons, which may be transferred from the SoxAX complex to another cytochrome c that then channels them into the respiratory electron transport chain. Some electrons may be used for reductive CO(2) fixation.<ref>PMID:10940005</ref> <ref>PMID:16297640</ref> <ref>PMID:17547421</ref>  
== 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>
[[Category: Atcc 17741]]
[[Category: Atcc 35512]]
[[Category: Large Structures]]
[[Category: Large Structures]]
[[Category: Dambe, T]]
[[Category: Paracoccus denitrificans]]
[[Category: Friedrich, C]]
[[Category: Paracoccus pantotrophus]]
[[Category: Quentmeier, A]]
[[Category: Dambe T]]
[[Category: Rother, D]]
[[Category: Friedrich C]]
[[Category: Scheidig, A J]]
[[Category: Quentmeier A]]
[[Category: Cytochrome-c-type]]
[[Category: Rother D]]
[[Category: Oxidoreductase]]
[[Category: Scheidig AJ]]
[[Category: Sulfur oxidation]]
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