2ebd
From Proteopedia
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<StructureSection load='2ebd' size='340' side='right'caption='[[2ebd]], [[Resolution|resolution]] 2.10Å' scene=''> | <StructureSection load='2ebd' size='340' side='right'caption='[[2ebd]], [[Resolution|resolution]] 2.10Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
| - | <table><tr><td colspan='2'>[[2ebd]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/ | + | <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=' | + | </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> |
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<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> | <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> | </table> | ||
== Function == | == 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 == | == Evolutionary Conservation == | ||
[[Image:Consurf_key_small.gif|200px|right]] | [[Image:Consurf_key_small.gif|200px|right]] | ||
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__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
| - | [[Category: | + | [[Category: Aquifex aeolicus VF5]] |
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
| - | [[Category: Kumarevel | + | [[Category: Kumarevel TS]] |
| - | [[Category: Kuramitsu | + | [[Category: Kuramitsu S]] |
| - | + | [[Category: Yokoyama S]] | |
| - | [[Category: Yokoyama | + | |
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Current revision
Crystal structure of 3-oxoacyl-[acyl-carrier-protein] synthase III from Aquifex aeolicus VF5
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