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New page: left|200px<br /> <applet load="1yb5" size="450" color="white" frame="true" align="right" spinBox="true" caption="1yb5, resolution 1.85Å" /> '''Crystal structure o...
 
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[[Image:1yb5.gif|left|200px]]<br />
<applet load="1yb5" size="450" color="white" frame="true" align="right" spinBox="true"
caption="1yb5, resolution 1.85&Aring;" />
'''Crystal structure of human Zeta-Crystallin with bound NADP'''<br />


==About this Structure==
==Crystal structure of human Zeta-Crystallin with bound NADP==
1YB5 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] with ACT, CL, NAP and GOL as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/NADPH:quinone_reductase NADPH:quinone reductase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.6.5.5 1.6.5.5] Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1YB5 OCA].  
<StructureSection load='1yb5' size='340' side='right'caption='[[1yb5]], [[Resolution|resolution]] 1.85&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[1yb5]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1YB5 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1YB5 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]] 1.85&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ACT:ACETATE+ION'>ACT</scene>, <scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=NAP:NADP+NICOTINAMIDE-ADENINE-DINUCLEOTIDE+PHOSPHATE'>NAP</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=1yb5 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1yb5 OCA], [https://pdbe.org/1yb5 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1yb5 RCSB], [https://www.ebi.ac.uk/pdbsum/1yb5 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1yb5 ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/QOR_HUMAN QOR_HUMAN] Does not have alcohol dehydrogenase activity. Binds NADP and acts through a one-electron transfer process. Orthoquinones, such as 1,2-naphthoquinone or 9,10-phenanthrenequinone, are the best substrates (in vitro). May act in the detoxification of xenobiotics. Interacts with (AU)-rich elements (ARE) in the 3'-UTR of target mRNA species. Enhances the stability of mRNA coding for BCL2. NADPH binding interferes with mRNA binding.<ref>PMID:17497241</ref> <ref>PMID:20103721</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/yb/1yb5_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=1yb5 ConSurf].
<div style="clear:both"></div>
 
==See Also==
*[[Quinone reductase 3D structures|Quinone reductase 3D structures]]
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
[[Category: NADPH:quinone reductase]]
[[Category: Large Structures]]
[[Category: Single protein]]
[[Category: Arrowsmith C]]
[[Category: Arrowsmith, C.]]
[[Category: Berridge G]]
[[Category: Berridge, G.]]
[[Category: Bray J]]
[[Category: Bray, J.]]
[[Category: Colbrook S]]
[[Category: Colbrook, S.]]
[[Category: Debreczeni J]]
[[Category: Debreczeni, J.]]
[[Category: Edwards A]]
[[Category: Delft, F.von.]]
[[Category: Gileadi O]]
[[Category: Edwards, A.]]
[[Category: Kavanagh K]]
[[Category: Gileadi, O.]]
[[Category: Oppermann U]]
[[Category: Kavanagh, K.]]
[[Category: Sundstrom M]]
[[Category: Oppermann, U.]]
[[Category: Williams L]]
[[Category: SGC, Structural.Genomics.Consortium.]]
[[Category: Von Delft F]]
[[Category: Sundstrom, M.]]
[[Category: Williams, L.]]
[[Category: ACT]]
[[Category: CL]]
[[Category: GOL]]
[[Category: NAP]]
[[Category: medium-chain dehydrogenase/reductase]]
[[Category: oxidoreductase]]
[[Category: quinone reduction]]
[[Category: sgc]]
[[Category: structural genomics]]
[[Category: structural genomics consortium]]
 
''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Mon Nov 12 20:17:29 2007''

Latest revision as of 08:56, 14 February 2024

Crystal structure of human Zeta-Crystallin with bound NADP

1yb5, resolution 1.85Å

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