3kd9: Difference between revisions
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==Crystal structure of pyridine nucleotide disulfide oxidoreductase from Pyrococcus horikoshii== | |||
<StructureSection load='3kd9' size='340' side='right'caption='[[3kd9]], [[Resolution|resolution]] 2.75Å' scene=''> | |||
== Structural highlights == | |||
<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> | |||
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.75Å</td></tr> | |||
== | <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> | ||
[[3kd9]] is a 3 chain structure | <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> | ||
</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> | |||
== Evolutionary Conservation == | |||
[[Image:Consurf_key_small.gif|200px|right]] | |||
Check<jmol> | |||
<jmolCheckbox> | |||
<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/kd/3kd9_consurf.spt"</scriptWhenChecked> | |||
<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> | |||
<text>to colour the structure by Evolutionary Conservation</text> | |||
</jmolCheckbox> | |||
</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=3kd9 ConSurf]. | |||
<div style="clear:both"></div> | |||
==See Also== | ==See Also== | ||
*[[Coenzyme A-Disulfide Reductase|Coenzyme A-Disulfide Reductase]] | *[[Coenzyme A-Disulfide Reductase|Coenzyme A-Disulfide Reductase]] | ||
[[Category: | == References == | ||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Large Structures]] | |||
[[Category: Pyrococcus horikoshii]] | [[Category: Pyrococcus horikoshii]] | ||
[[Category: Agarwal | [[Category: Agarwal R]] | ||
[[Category: Burley | [[Category: Burley SK]] | ||
[[Category: Swaminathan S]] | |||
[[Category: Swaminathan | |||
Latest revision as of 13:16, 21 February 2024
Crystal structure of pyridine nucleotide disulfide oxidoreductase from Pyrococcus horikoshiiCrystal structure of pyridine nucleotide disulfide oxidoreductase from Pyrococcus horikoshii
Structural highlights
FunctionNCPPR_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).[1] [2] Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. See AlsoReferences
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