2xts: Difference between revisions

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== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[2xts]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Paracoccus_pantotrophus Paracoccus pantotrophus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2XTS OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2XTS FirstGlance]. <br>
<table><tr><td colspan='2'>[[2xts]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Paracoccus_pantotrophus Paracoccus pantotrophus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2XTS OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2XTS FirstGlance]. <br>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=2MO:MOLYBDENUM+(IV)OXIDE'>2MO</scene>, <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=CO:COBALT+(II)+ION'>CO</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=HEC:HEME+C'>HEC</scene>, <scene name='pdbligand=MTE:PHOSPHONIC+ACIDMONO-(2-AMINO-5,6-DIMERCAPTO-4-OXO-3,7,8A,9,10,10A-HEXAHYDRO-4H-8-OXA-1,3,9,10-TETRAAZA-ANTHRACEN-7-YLMETHYL)ESTER'>MTE</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]] 1.33&#8491;</td></tr>
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[1wq0|1wq0]]</div></td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=2MO:MOLYBDENUM+(IV)OXIDE'>2MO</scene>, <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=CO:COBALT+(II)+ION'>CO</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=HEC:HEME+C'>HEC</scene>, <scene name='pdbligand=MTE:PHOSPHONIC+ACIDMONO-(2-AMINO-5,6-DIMERCAPTO-4-OXO-3,7,8A,9,10,10A-HEXAHYDRO-4H-8-OXA-1,3,9,10-TETRAAZA-ANTHRACEN-7-YLMETHYL)ESTER'>MTE</scene></td></tr>
<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/Sulfite_dehydrogenase Sulfite dehydrogenase], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.8.2.1 1.8.2.1] </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=2xts FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2xts OCA], [https://pdbe.org/2xts PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2xts RCSB], [https://www.ebi.ac.uk/pdbsum/2xts PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2xts 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=2xts FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2xts OCA], [https://pdbe.org/2xts PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2xts RCSB], [https://www.ebi.ac.uk/pdbsum/2xts PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2xts ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
[[https://www.uniprot.org/uniprot/P72178_PARDE P72178_PARDE]] The exact function is not known. Can catalyze the reduction of a variety of substrates like dimethyl sulfoxide, trimethylamine N-oxide, phenylmethyl sulfoxide and L-methionine sulfoxide. Cannot reduce cyclic N-oxides. Shows no activity as sulfite oxidase.[SAAS:SAAS00086612]  
[https://www.uniprot.org/uniprot/P72178_PARDE P72178_PARDE] The exact function is not known. Can catalyze the reduction of a variety of substrates like dimethyl sulfoxide, trimethylamine N-oxide, phenylmethyl sulfoxide and L-methionine sulfoxide. Cannot reduce cyclic N-oxides. Shows no activity as sulfite oxidase.[SAAS:SAAS00086612]
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== Publication Abstract from PubMed ==
== Publication Abstract from PubMed ==
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[[Category: Large Structures]]
[[Category: Large Structures]]
[[Category: Paracoccus pantotrophus]]
[[Category: Paracoccus pantotrophus]]
[[Category: Sulfite dehydrogenase]]
[[Category: Bardischewski F]]
[[Category: Bardischewski, F]]
[[Category: Faust A]]
[[Category: Faust, A]]
[[Category: Friedrich CG]]
[[Category: Friedrich, C G]]
[[Category: Klink BU]]
[[Category: Klink, B U]]
[[Category: Panjikar S]]
[[Category: Panjikar, S]]
[[Category: Quentmeier A]]
[[Category: Quentmeier, A]]
[[Category: Scheidig AJ]]
[[Category: Sanctis, D de]]
[[Category: Zander U]]
[[Category: Scheidig, A J]]
[[Category: De Sanctis D]]
[[Category: Zander, U]]
[[Category: Electron transfer]]
[[Category: Heme]]
[[Category: Molybdenum cofactor]]
[[Category: Oxidoreductase-electron transport complex]]
[[Category: Sox system]]
[[Category: Sulfane oxidation]]