4fx9
From Proteopedia
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| - | '''Unreleased structure''' | ||
| - | + | ==Structure of the Pyrococcus horikoshii CoA persulfide/polysulfide reductase== | |
| + | <StructureSection load='4fx9' size='340' side='right'caption='[[4fx9]], [[Resolution|resolution]] 2.70Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[4fx9]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Pyrococcus_horikoshii_OT3 Pyrococcus horikoshii OT3]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4FX9 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4FX9 FirstGlance]. <br> | ||
| + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.7Å</td></tr> | ||
| + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=COA:COENZYME+A'>COA</scene>, <scene name='pdbligand=FAD:FLAVIN-ADENINE+DINUCLEOTIDE'>FAD</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=4fx9 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4fx9 OCA], [https://pdbe.org/4fx9 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4fx9 RCSB], [https://www.ebi.ac.uk/pdbsum/4fx9 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4fx9 ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | == Function == | ||
| + | [https://www.uniprot.org/uniprot/NCPPR_PYRHO NCPPR_PYRHO] Catalyzes the NAD(P)H-dependent reduction of polysulfide, CoA-polysulfides, and CoA persulfide, as well as the reduction of a range of other small persulfides, including TNB and glutathione persulfides. The likely in vivo substrates are di-, poly-, and persulfide derivatives of coenzyme A, although polysulfide itself is also efficiently reduced (PubMed:23530771). Shows coenzyme A disulfide reductase (CoADR) activity with both NADH and NADPH, with a preference for NADPH (PubMed:15720393). May also play a role in the reduction of elemental sulfur (PubMed:23530771).<ref>PMID:15720393</ref> <ref>PMID:23530771</ref> | ||
| - | + | ==See Also== | |
| - | + | *[[Coenzyme A-Disulfide Reductase|Coenzyme A-Disulfide Reductase]] | |
| - | + | == References == | |
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Large Structures]] | ||
| + | [[Category: Pyrococcus horikoshii OT3]] | ||
| + | [[Category: Crane III EJ]] | ||
| + | [[Category: Herwald S]] | ||
| + | [[Category: Lopez KM]] | ||
| + | [[Category: Sazinsky MH]] | ||
Current revision
Structure of the Pyrococcus horikoshii CoA persulfide/polysulfide reductase
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