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[[Image:1asa.gif|left|200px]]


{{Structure
==THE STRUCTURAL BASIS FOR THE REDUCED ACTIVITY OF THE Y226F(Y225F) ACTIVE SITE MUTANT OF E. COLI ASPARTATE AMINOTRANSFERASE==
|PDB= 1asa |SIZE=350|CAPTION= <scene name='initialview01'>1asa</scene>, resolution 2.4&Aring;
<StructureSection load='1asa' size='340' side='right'caption='[[1asa]], [[Resolution|resolution]] 2.40&Aring;' scene=''>
|SITE=  
== Structural highlights ==
|LIGAND= <scene name='pdbligand=PLP:PYRIDOXAL-5'-PHOSPHATE'>PLP</scene> and <scene name='pdbligand=MAE:MALEIC ACID'>MAE</scene>
<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>
|ACTIVITY= [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]  
</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>
|GENE=  
<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>


'''THE STRUCTURAL BASIS FOR THE REDUCED ACTIVITY OF THE Y226F(Y225F) ACTIVE SITE MUTANT OF E. COLI ASPARTATE AMINOTRANSFERASE'''
==See Also==
 
*[[Aspartate aminotransferase 3D structures|Aspartate aminotransferase 3D structures]]
 
__TOC__
==About this Structure==
</StructureSection>
1ASA is a [[Single protein]] structure of sequence from [http://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].
[[Category: Aspartate transaminase]]
[[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://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 10:01:40 2008''

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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