2ebd: Difference between revisions
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New page: left|200px<br /><applet load="2ebd" size="350" color="white" frame="true" align="right" spinBox="true" caption="2ebd, resolution 2.10Å" /> '''Crystal structure of... |
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== | ==Crystal structure of 3-oxoacyl-[acyl-carrier-protein] synthase III from Aquifex aeolicus VF5== | ||
<StructureSection load='2ebd' size='340' side='right'caption='[[2ebd]], [[Resolution|resolution]] 2.10Å' scene=''> | |||
[ | == Structural highlights == | ||
[ | <table><tr><td colspan='2'>[[2ebd]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Aquifex_aeolicus_VF5 Aquifex aeolicus VF5]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2EBD OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2EBD 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]] 2.1Å</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=2ebd FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2ebd OCA], [https://pdbe.org/2ebd PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2ebd RCSB], [https://www.ebi.ac.uk/pdbsum/2ebd PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2ebd ProSAT], [https://www.topsan.org/Proteins/RSGI/2ebd TOPSAN]</span></td></tr> | |||
</table> | |||
[ | == Function == | ||
[ | [https://www.uniprot.org/uniprot/FABH_AQUAE FABH_AQUAE] Catalyzes the condensation reaction of fatty acid synthesis by the addition to an acyl acceptor of two carbons from malonyl-ACP. Catalyzes the first condensation reaction which initiates fatty acid synthesis and may therefore play a role in governing the total rate of fatty acid production. Possesses both acetoacetyl-ACP synthase and acetyl transacylase activities. Its substrate specificity determines the biosynthesis of branched-chain and/or straight-chain of fatty acids (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/eb/2ebd_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=2ebd ConSurf]. | ||
[ | <div style="clear:both"></div> | ||
==See Also== | |||
*[[Acyl carrier protein synthase 3D structures|Acyl carrier protein synthase 3D structures]] | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Aquifex aeolicus VF5]] | |||
[[Category: Large Structures]] | |||
[[Category: Kumarevel TS]] | |||
[[Category: Kuramitsu S]] | |||
[[Category: Yokoyama S]] | |||
Latest revision as of 11:38, 25 October 2023
Crystal structure of 3-oxoacyl-[acyl-carrier-protein] synthase III from Aquifex aeolicus VF5Crystal structure of 3-oxoacyl-[acyl-carrier-protein] synthase III from Aquifex aeolicus VF5
Structural highlights
FunctionFABH_AQUAE Catalyzes the condensation reaction of fatty acid synthesis by the addition to an acyl acceptor of two carbons from malonyl-ACP. Catalyzes the first condensation reaction which initiates fatty acid synthesis and may therefore play a role in governing the total rate of fatty acid production. Possesses both acetoacetyl-ACP synthase and acetyl transacylase activities. Its substrate specificity determines the biosynthesis of branched-chain and/or straight-chain of fatty acids (By similarity). 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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