1nel: Difference between revisions

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[[Image:1nel.png|left|200px]]


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==FLUORIDE INHIBITION OF YEAST ENOLASE: CRYSTAL STRUCTURE OF THE ENOLASE-MG2+-F--PI COMPLEX AT 2.6-ANGSTROMS RESOLUTION==
The line below this paragraph, containing "STRUCTURE_1nel", creates the "Structure Box" on the page.
<StructureSection load='1nel' size='340' side='right'caption='[[1nel]], [[Resolution|resolution]] 2.60&Aring;' scene=''>
You may change the PDB parameter (which sets the PDB file loaded into the applet)
== Structural highlights ==
or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
<table><tr><td colspan='2'>[[1nel]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1NEL OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1NEL FirstGlance]. <br>
or leave the SCENE parameter empty for the default display.
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.6&#8491;</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=F:FLUORIDE+ION'>F</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene></td></tr>
{{STRUCTURE_1nel| PDB=1nel |  SCENE= }}
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1nel FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1nel OCA], [https://pdbe.org/1nel PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1nel RCSB], [https://www.ebi.ac.uk/pdbsum/1nel PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1nel ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/ENO1_YEAST ENO1_YEAST]
== 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/ne/1nel_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=1nel ConSurf].
<div style="clear:both"></div>


===FLUORIDE INHIBITION OF YEAST ENOLASE: CRYSTAL STRUCTURE OF THE ENOLASE-MG2+-F--PI COMPLEX AT 2.6-ANGSTROMS RESOLUTION===
==See Also==
 
*[[Enolase 3D structures|Enolase 3D structures]]
 
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The line below this paragraph, {{ABSTRACT_PUBMED_8346189}}, adds the Publication Abstract to the page
[[Category: Large Structures]]
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{{ABSTRACT_PUBMED_8346189}}
 
==About this Structure==
1NEL is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1NEL OCA].
 
==Reference==
Fluoride inhibition of yeast enolase: crystal structure of the enolase-Mg(2+)-F(-)-Pi complex at 2.6 A resolution., Lebioda L, Zhang E, Lewinski K, Brewer JM, Proteins. 1993 Jul;16(3):219-25. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/8346189 8346189]
[[Category: Phosphopyruvate hydratase]]
[[Category: Saccharomyces cerevisiae]]
[[Category: Saccharomyces cerevisiae]]
[[Category: Single protein]]
[[Category: Brewer MJ]]
[[Category: Brewer, M J.]]
[[Category: Lebioda L]]
[[Category: Lebioda, L.]]
[[Category: Lewinski K]]
[[Category: Lewinski, K.]]
[[Category: Zhang E]]
[[Category: Zhang, E.]]
[[Category: Carbon-oxygen lyase]]
 
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