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[[Image:3b97.png|left|200px]]


{{STRUCTURE_3b97|  PDB=3b97  |  SCENE=  }}
==Crystal Structure of human Enolase 1==
 
<StructureSection load='3b97' size='340' side='right'caption='[[3b97]], [[Resolution|resolution]] 2.20&Aring;' scene=''>
===Crystal Structure of human Enolase 1===
== Structural highlights ==
 
<table><tr><td colspan='2'>[[3b97]] is a 4 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=3B97 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3B97 FirstGlance]. <br>
{{ABSTRACT_PUBMED_18560153}}
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.2&#8491;</td></tr>
 
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>
==About this Structure==
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=3b97 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3b97 OCA], [https://pdbe.org/3b97 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3b97 RCSB], [https://www.ebi.ac.uk/pdbsum/3b97 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3b97 ProSAT]</span></td></tr>
[[3b97]] is a 4 chain structure of [[Enolase]] with sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3B97 OCA].  
</table>
== Function ==
[https://www.uniprot.org/uniprot/ENOA_HUMAN ENOA_HUMAN] Multifunctional enzyme that, as well as its role in glycolysis, plays a part in various processes such as growth control, hypoxia tolerance and allergic responses. May also function in the intravascular and pericellular fibrinolytic system due to its ability to serve as a receptor and activator of plasminogen on the cell surface of several cell-types such as leukocytes and neurons. Stimulates immunoglobulin production.<ref>PMID:2005901</ref> <ref>PMID:1369209</ref> <ref>PMID:10082554</ref> <ref>PMID:10802057</ref> <ref>PMID:12666133</ref>  MBP1 binds to the myc promoter and acts as a transcriptional repressor. May be a tumor suppressor.<ref>PMID:2005901</ref> <ref>PMID:1369209</ref> <ref>PMID:10082554</ref> <ref>PMID:10802057</ref> <ref>PMID:12666133</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/b9/3b97_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=3b97 ConSurf].
<div style="clear:both"></div>


==See Also==
==See Also==
*[[Enolase|Enolase]]
*[[Enolase 3D structures|Enolase 3D structures]]
 
== References ==
==Reference==
<references/>
<ref group="xtra">PMID:018560153</ref><references group="xtra"/>
__TOC__
</StructureSection>
[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
[[Category: Phosphopyruvate hydratase]]
[[Category: Large Structures]]
[[Category: Chung, S J.]]
[[Category: Chung SJ]]
[[Category: Jung, S K.]]
[[Category: Jung SK]]
[[Category: Kang, H J.]]
[[Category: Kang HJ]]
[[Category: Kim, S J.]]
[[Category: Kim SJ]]
[[Category: Alpha/beta hydrolase]]
[[Category: Alternative initiation]]
[[Category: Dna-binding]]
[[Category: Glycolysis]]
[[Category: Lyase]]
[[Category: Magnesium]]
[[Category: Membrane]]
[[Category: Metal-binding]]
[[Category: Nucleus]]
[[Category: Phosphorylation]]
[[Category: Plasminogen activation]]
[[Category: Repressor]]
[[Category: Transcription]]
[[Category: Transcription regulation]]

Latest revision as of 14:03, 13 March 2024

Crystal Structure of human Enolase 1

3b97, resolution 2.20Å

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