1idd: Difference between revisions

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{{Seed}}
[[Image:1idd.png|left|200px]]


<!--
==ISOCITRATE DEHYDROGENASE Y160F MUTANT APO ENZYME==
The line below this paragraph, containing "STRUCTURE_1idd", creates the "Structure Box" on the page.
<StructureSection load='1idd' size='340' side='right'caption='[[1idd]], [[Resolution|resolution]] 2.50&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'>[[1idd]] 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=1IDD OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1IDD 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]] 2.5&#8491;</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=1idd FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1idd OCA], [https://pdbe.org/1idd PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1idd RCSB], [https://www.ebi.ac.uk/pdbsum/1idd PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1idd ProSAT]</span></td></tr>
{{STRUCTURE_1idd|  PDB=1idd |  SCENE= }}
</table>
== Function ==
[https://www.uniprot.org/uniprot/IDH_ECOLI IDH_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/id/1idd_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=1idd ConSurf].
<div style="clear:both"></div>


===ISOCITRATE DEHYDROGENASE Y160F MUTANT APO ENZYME===
==See Also==
 
*[[Isocitrate dehydrogenase 3D structures|Isocitrate dehydrogenase 3D structures]]
 
__TOC__
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</StructureSection>
The line below this paragraph, {{ABSTRACT_PUBMED_7819221}}, adds the Publication Abstract to the page
(as it appears on PubMed at http://www.pubmed.gov), where 7819221 is the PubMed ID number.
-->
{{ABSTRACT_PUBMED_7819221}}
 
==About this Structure==
1IDD 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=1IDD OCA].
 
==Reference==
Mutational analysis of the catalytic residues lysine 230 and tyrosine 160 in the NADP(+)-dependent isocitrate dehydrogenase from Escherichia coli., Lee ME, Dyer DH, Klein OD, Bolduc JM, Stoddard BL, Koshland DE Jr, Biochemistry. 1995 Jan 10;34(1):378-84. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/7819221 7819221]
[[Category: Escherichia coli]]
[[Category: Escherichia coli]]
[[Category: Single protein]]
[[Category: Large Structures]]
[[Category: Bolduc, J M.]]
[[Category: Bolduc JM]]
[[Category: Dyer, D H.]]
[[Category: Dyer DH]]
[[Category: Junior, D E.Koshland.]]
[[Category: Klein OD]]
[[Category: Klein, O D.]]
[[Category: Koshland Junior DE]]
[[Category: Lee, M E.]]
[[Category: Lee ME]]
[[Category: Stoddard, B L.]]
[[Category: Stoddard BL]]
 
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul  1 10:47:49 2008''

Latest revision as of 07:34, 7 February 2024

ISOCITRATE DEHYDROGENASE Y160F MUTANT APO ENZYME

1idd, resolution 2.50Å

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