3kd9

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==Crystal structure of pyridine nucleotide disulfide oxidoreductase from Pyrococcus horikoshii==
==Crystal structure of pyridine nucleotide disulfide oxidoreductase from Pyrococcus horikoshii==
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<StructureSection load='3kd9' size='340' side='right' caption='[[3kd9]], [[Resolution|resolution]] 2.75&Aring;' scene=''>
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<StructureSection load='3kd9' size='340' side='right'caption='[[3kd9]], [[Resolution|resolution]] 2.75&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[3kd9]] is a 3 chain structure with sequence from [http://en.wikipedia.org/wiki/'pyrococcus_shinkaii' 'pyrococcus shinkaii']. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3KD9 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3KD9 FirstGlance]. <br>
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<table><tr><td colspan='2'>[[3kd9]] is a 3 chain structure with sequence from [https://en.wikipedia.org/wiki/Pyrococcus_horikoshii Pyrococcus horikoshii]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3KD9 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3KD9 FirstGlance]. <br>
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</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</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]] 2.75&#8491;</td></tr>
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<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">PH0572 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=53953 'Pyrococcus shinkaii'])</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=GOL:GLYCEROL'>GOL</scene></td></tr>
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<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/CoA-disulfide_reductase CoA-disulfide reductase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.8.1.14 1.8.1.14] </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=3kd9 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3kd9 OCA], [https://pdbe.org/3kd9 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3kd9 RCSB], [https://www.ebi.ac.uk/pdbsum/3kd9 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3kd9 ProSAT]</span></td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3kd9 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3kd9 OCA], [http://pdbe.org/3kd9 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3kd9 RCSB], [http://www.ebi.ac.uk/pdbsum/3kd9 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3kd9 ProSAT]</span></td></tr>
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</table>
</table>
== Function ==
== Function ==
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[[http://www.uniprot.org/uniprot/CDR_PYRHO CDR_PYRHO]] Acts as a coenzyme A disulfide reductase. Specific for CoA disulfide. Shows a slow NAD(P)H oxidase activity in the presence of high concentrations of substrate-level FAD. This demonstrates that it is not likely to act as an NADH oxidase in vivo.
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[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>
== Evolutionary Conservation ==
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
[[Image:Consurf_key_small.gif|200px|right]]
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==See Also==
==See Also==
*[[Coenzyme A-Disulfide Reductase|Coenzyme A-Disulfide Reductase]]
*[[Coenzyme A-Disulfide Reductase|Coenzyme A-Disulfide Reductase]]
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== References ==
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<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: Pyrococcus shinkaii]]
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[[Category: Large Structures]]
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[[Category: CoA-disulfide reductase]]
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[[Category: Pyrococcus horikoshii]]
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[[Category: Agarwal, R]]
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[[Category: Agarwal R]]
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[[Category: Burley, S K]]
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[[Category: Burley SK]]
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[[Category: Structural genomic]]
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[[Category: Swaminathan S]]
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[[Category: Swaminathan, S]]
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[[Category: Fad]]
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[[Category: Flavoprotein]]
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[[Category: Nad]]
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[[Category: NYSGXRC, New York SGX Research Center for Structural Genomics]]
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[[Category: Oxidoreductase]]
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[[Category: PSI, Protein structure initiative]]
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[[Category: Redox-active center]]
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Current revision

Crystal structure of pyridine nucleotide disulfide oxidoreductase from Pyrococcus horikoshii

PDB ID 3kd9

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