1xmd: Difference between revisions

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


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==M335V mutant structure of mouse carnitine octanoyltransferase==
The line below this paragraph, containing "STRUCTURE_1xmd", creates the "Structure Box" on the page.
<StructureSection load='1xmd' size='340' side='right'caption='[[1xmd]], [[Resolution|resolution]] 2.10&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'>[[1xmd]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1XMD OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1XMD 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]] 2.1&#8491;</td></tr>
-->
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=EPE:4-(2-HYDROXYETHYL)-1-PIPERAZINE+ETHANESULFONIC+ACID'>EPE</scene>, <scene name='pdbligand=MPD:(4S)-2-METHYL-2,4-PENTANEDIOL'>MPD</scene></td></tr>
{{STRUCTURE_1xmd| PDB=1xmd |  SCENE= }}
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1xmd FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1xmd OCA], [https://pdbe.org/1xmd PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1xmd RCSB], [https://www.ebi.ac.uk/pdbsum/1xmd PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1xmd ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/OCTC_MOUSE OCTC_MOUSE] Beta-oxidation of fatty acids. The highest activity concerns the C6 to C10 chain length substrate (By similarity).
== 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/xm/1xmd_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=1xmd ConSurf].
<div style="clear:both"></div>


===M335V mutant structure of mouse carnitine octanoyltransferase===
==See Also==
 
*[[Butyrylcholinesterase 3D structures|Butyrylcholinesterase 3D structures]]
 
__TOC__
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</StructureSection>
The line below this paragraph, {{ABSTRACT_PUBMED_15492013}}, adds the Publication Abstract to the page
[[Category: Large Structures]]
(as it appears on PubMed at http://www.pubmed.gov), where 15492013 is the PubMed ID number.
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{{ABSTRACT_PUBMED_15492013}}
 
==About this Structure==
1XMD is a 2 chains structure of sequences from [http://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1XMD OCA].
 
==Reference==
<ref group="xtra">PMID:15492013</ref><references group="xtra"/>
[[Category: Carnitine O-octanoyltransferase]]
[[Category: Mus musculus]]
[[Category: Mus musculus]]
[[Category: Hsiao, Y S.]]
[[Category: Hsiao YS]]
[[Category: Jogl, G.]]
[[Category: Jogl G]]
[[Category: Tong, L.]]
[[Category: Tong L]]
[[Category: Carnitine]]
[[Category: Hepe]]
[[Category: Mpd]]
[[Category: Mutant]]
[[Category: Octanoyltransferase]]
 
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Feb 17 02:16:22 2009''