2ebd
From Proteopedia
(Difference between revisions)
(New page: 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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| - | [[Image:2ebd.jpg|left|200px]]<br /><applet load="2ebd" size="350" color="white" frame="true" align="right" spinBox="true" | ||
| - | caption="2ebd, resolution 2.10Å" /> | ||
| - | '''Crystal structure of 3-oxoacyl-[acyl-carrier-protein] synthase III from Aquifex aeolicus VF5'''<br /> | ||
| - | == | + | ==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]] | ||
Current revision
Crystal structure of 3-oxoacyl-[acyl-carrier-protein] synthase III from Aquifex aeolicus VF5
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