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3enl

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[[Image:3enl.jpg|left|200px]]
 
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{{Structure
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==REFINED STRUCTURE OF YEAST APO-ENOLASE AT 2.25 ANGSTROMS RESOLUTION==
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|PDB= 3enl |SIZE=350|CAPTION= <scene name='initialview01'>3enl</scene>, resolution 2.25&Aring;
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<StructureSection load='3enl' size='340' side='right'caption='[[3enl]], [[Resolution|resolution]] 2.25&Aring;' scene=''>
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|SITE=
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== Structural highlights ==
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|LIGAND= <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene>
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<table><tr><td colspan='2'>[[3enl]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae]. This structure supersedes the now removed PDB entries [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=2enl 2enl] and [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=1enl 1enl]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3ENL OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3ENL FirstGlance]. <br>
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|ACTIVITY= <span class='plainlinks'>[http://en.wikipedia.org/wiki/Phosphopyruvate_hydratase Phosphopyruvate hydratase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=4.2.1.11 4.2.1.11] </span>
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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]] 2.25&#8491;</td></tr>
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|GENE=
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>
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|DOMAIN=
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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=3enl FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3enl OCA], [https://pdbe.org/3enl PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3enl RCSB], [https://www.ebi.ac.uk/pdbsum/3enl PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3enl ProSAT]</span></td></tr>
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|RELATEDENTRY=
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</table>
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3enl FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3enl OCA], [http://www.ebi.ac.uk/pdbsum/3enl PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=3enl RCSB]</span>
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== Function ==
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}}
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[https://www.uniprot.org/uniprot/ENO1_YEAST ENO1_YEAST]
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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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Check<jmol>
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<jmolCheckbox>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/en/3enl_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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</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=3enl ConSurf].
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<div style="clear:both"></div>
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'''REFINED STRUCTURE OF YEAST APO-ENOLASE AT 2.25 ANGSTROMS RESOLUTION'''
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==See Also==
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*[[Enolase 3D structures|Enolase 3D structures]]
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__TOC__
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==Overview==
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</StructureSection>
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The crystal structure of apo-enolase from baker's yeast (Saccharomyces cerevisiae) was established at 2.25 A resolution using a restrained least-squares refinement method. Based on 21,077 independent reflections of better than 8 A resolution, a final R-factor of 15.4% was obtained with a model obeying standard geometry within 0.017 A in bond length and 3.5 degrees in bond angles. The upper limit for the co-ordinate accuracy of the atoms was estimated to be 0.18 A. The refinement confirmed the heterodox, non-parallel character of the 8-fold beta alpha-barrel domain with beta beta alpha alpha(beta alpha)6 topology. The reported structure for which the data were collected at pH 5.0 represents an apo-form of the enzyme. Of the three carboxylic ligands that form the conformational metal ion binding site two, Glu295 and Asp320, are very close and presumably form a strong acidic type hydrogen bond with the proton partially replacing the electric charge of the physiological cofactor Mg2+. The single sulfate ion found in the structure is in the active site cavity, co-ordinated to the side-chains of Lys345 and Arg374, and to the N atom of Ser375. It is located about 7.4 A from the conformational metal ion binding site. It occupies the site in which the phosphate group of the substrate binds.
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[[Category: Large Structures]]
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==About this Structure==
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3ENL is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae]. This structure supersedes the now removed PDB entries 2ENL and 1ENL. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3ENL OCA].
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==Reference==
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Refined structure of yeast apo-enolase at 2.25 A resolution., Stec B, Lebioda L, J Mol Biol. 1990 Jan 5;211(1):235-48. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/2405163 2405163]
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[[Category: Phosphopyruvate hydratase]]
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[[Category: Saccharomyces cerevisiae]]
[[Category: Saccharomyces cerevisiae]]
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[[Category: Single protein]]
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[[Category: Lebioda L]]
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[[Category: Lebioda, L.]]
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[[Category: Stec B]]
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[[Category: Stec, B.]]
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[[Category: carbon-oxygen lyase]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 05:33:09 2008''
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Current revision

REFINED STRUCTURE OF YEAST APO-ENOLASE AT 2.25 ANGSTROMS RESOLUTION

PDB ID 3enl

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