2qht: Difference between revisions

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New page: left|200px<br /><applet load="2qht" size="350" color="white" frame="true" align="right" spinBox="true" caption="2qht, resolution 1.500Å" /> '''Structural Basis of...
 
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[[Image:2qht.jpg|left|200px]]<br /><applet load="2qht" size="350" color="white" frame="true" align="right" spinBox="true"
caption="2qht, resolution 1.500&Aring;" />
'''Structural Basis of Octanoic Acid Recognition by Lipoate-Protein Ligase B'''<br />


==About this Structure==
==Structural Basis of Octanoic Acid Recognition by Lipoate-Protein Ligase B==
2QHT is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Thermus_thermophilus Thermus thermophilus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2QHT OCA].  
<StructureSection load='2qht' size='340' side='right'caption='[[2qht]], [[Resolution|resolution]] 1.50&Aring;' scene=''>
 
== Structural highlights ==
==Reference==
<table><tr><td colspan='2'>[[2qht]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Thermus_thermophilus_HB8 Thermus thermophilus HB8]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2QHT OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2QHT FirstGlance]. <br>
Structural basis of octanoic acid recognition by lipoate-protein ligase B., Kim DJ, Lee SJ, Kim HS, Kim KH, Lee HH, Yoon HJ, Suh SW, Proteins. 2007 Dec 12;70(4):1620-1625. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=18076036 18076036]
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.5&#8491;</td></tr>
[[Category: Single protein]]
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2qht FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2qht OCA], [https://pdbe.org/2qht PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2qht RCSB], [https://www.ebi.ac.uk/pdbsum/2qht PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2qht ProSAT]</span></td></tr>
[[Category: Thermus thermophilus]]
</table>
[[Category: Kim, D J.]]
== Function ==
[[Category: Kim, H S.]]
[https://www.uniprot.org/uniprot/LIPB_THET8 LIPB_THET8] Catalyzes the transfer of endogenously produced octanoic acid from octanoyl-acyl-carrier-protein onto the lipoyl domains of lipoate-dependent enzymes. Lipoyl-ACP can also act as a substrate although octanoyl-ACP is likely to be the physiological substrate (By similarity).
[[Category: Kim, K H.]]
== Evolutionary Conservation ==
[[Category: Lee, H H.]]
[[Image:Consurf_key_small.gif|200px|right]]
[[Category: Lee, S J.]]
Check<jmol>
[[Category: Suh, S W.]]
  <jmolCheckbox>
[[Category: Yoon, H J.]]
    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/qh/2qht_consurf.spt"</scriptWhenChecked>
[[Category: globular protein]]
    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
[[Category: transferase]]
    <text>to colour the structure by Evolutionary Conservation</text>
 
  </jmolCheckbox>
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Feb 27 07:58:57 2008''
</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=2qht ConSurf].
<div style="clear:both"></div>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Thermus thermophilus HB8]]
[[Category: Kim DJ]]
[[Category: Kim HS]]
[[Category: Kim KH]]
[[Category: Lee HH]]
[[Category: Lee SJ]]
[[Category: Suh SW]]
[[Category: Yoon HJ]]

Latest revision as of 13:54, 13 March 2024

Structural Basis of Octanoic Acid Recognition by Lipoate-Protein Ligase B

2qht, resolution 1.50Å

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