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New page: left|200px<br /><applet load="1asa" size="450" color="white" frame="true" align="right" spinBox="true" caption="1asa, resolution 2.4Å" /> '''THE STRUCTURAL BASIS ...
 
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[[Image:1asa.gif|left|200px]]<br /><applet load="1asa" size="450" color="white" frame="true" align="right" spinBox="true"
caption="1asa, resolution 2.4&Aring;" />
'''THE STRUCTURAL BASIS FOR THE REDUCED ACTIVITY OF THE Y226F(Y225F) ACTIVE SITE MUTANT OF E. COLI ASPARTATE AMINOTRANSFERASE'''<br />


==About this Structure==
==THE STRUCTURAL BASIS FOR THE REDUCED ACTIVITY OF THE Y226F(Y225F) ACTIVE SITE MUTANT OF E. COLI ASPARTATE AMINOTRANSFERASE==
1ASA is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli] with PLP and MAE as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/Aspartate_transaminase Aspartate transaminase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.6.1.1 2.6.1.1] Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1ASA OCA].  
<StructureSection load='1asa' size='340' side='right'caption='[[1asa]], [[Resolution|resolution]] 2.40&Aring;' scene=''>
[[Category: Aspartate transaminase]]
== Structural highlights ==
<table><tr><td colspan='2'>[[1asa]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1ASA OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1ASA 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]] 2.4&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MAE:MALEIC+ACID'>MAE</scene>, <scene name='pdbligand=PLP:PYRIDOXAL-5-PHOSPHATE'>PLP</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=1asa FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1asa OCA], [https://pdbe.org/1asa PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1asa RCSB], [https://www.ebi.ac.uk/pdbsum/1asa PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1asa ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/AAT_ECOLI AAT_ECOLI]
== 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/as/1asa_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=1asa ConSurf].
<div style="clear:both"></div>
 
==See Also==
*[[Aspartate aminotransferase 3D structures|Aspartate aminotransferase 3D structures]]
__TOC__
</StructureSection>
[[Category: Escherichia coli]]
[[Category: Escherichia coli]]
[[Category: Single protein]]
[[Category: Large Structures]]
[[Category: Ringe, D.]]
[[Category: Ringe D]]
[[Category: Schumacher, C.]]
[[Category: Schumacher C]]
[[Category: MAE]]
[[Category: PLP]]
[[Category: aminotransferase]]
 
''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 11:05:46 2007''

Latest revision as of 15:27, 13 March 2024

THE STRUCTURAL BASIS FOR THE REDUCED ACTIVITY OF THE Y226F(Y225F) ACTIVE SITE MUTANT OF E. COLI ASPARTATE AMINOTRANSFERASE

1asa, resolution 2.40Å

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