1xkt: Difference between revisions
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==Human fatty acid synthase: Structure and substrate selectivity of the thioesterase domain== | |||
<StructureSection load='1xkt' size='340' side='right'caption='[[1xkt]], [[Resolution|resolution]] 2.60Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[1xkt]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1XKT OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1XKT 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]] 2.6Å</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=1xkt FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1xkt OCA], [https://pdbe.org/1xkt PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1xkt RCSB], [https://www.ebi.ac.uk/pdbsum/1xkt PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1xkt ProSAT]</span></td></tr> | |||
== | </table> | ||
[[1xkt]] is a 2 chain structure | == Function == | ||
[https://www.uniprot.org/uniprot/FAS_HUMAN FAS_HUMAN] Fatty acid synthetase catalyzes the formation of long-chain fatty acids from acetyl-CoA, malonyl-CoA and NADPH. This multifunctional protein has 7 catalytic activities and an acyl carrier protein. | |||
== 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/xk/1xkt_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=1xkt ConSurf]. | |||
<div style="clear:both"></div> | |||
==See Also== | ==See Also== | ||
*[[Fatty acid synthase|Fatty acid synthase]] | *[[Fatty acid synthase 3D structures|Fatty acid synthase 3D structures]] | ||
__TOC__ | |||
</StructureSection> | |||
[[Category: Homo sapiens]] | [[Category: Homo sapiens]] | ||
[[Category: Chakravarty | [[Category: Large Structures]] | ||
[[Category: Chirala | [[Category: Chakravarty B]] | ||
[[Category: Gu | [[Category: Chirala SS]] | ||
[[Category: Quiocho | [[Category: Gu Z]] | ||
[[Category: Wakil | [[Category: Quiocho FA]] | ||
[[Category: Wakil SJ]] | |||
Latest revision as of 11:51, 14 February 2024
Human fatty acid synthase: Structure and substrate selectivity of the thioesterase domainHuman fatty acid synthase: Structure and substrate selectivity of the thioesterase domain
Structural highlights
FunctionFAS_HUMAN Fatty acid synthetase catalyzes the formation of long-chain fatty acids from acetyl-CoA, malonyl-CoA and NADPH. This multifunctional protein has 7 catalytic activities and an acyl carrier protein. Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. See Also |
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