3goa
From Proteopedia
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==Crystal structure of the Salmonella typhimurium FadA 3-ketoacyl-CoA thiolase== | ==Crystal structure of the Salmonella typhimurium FadA 3-ketoacyl-CoA thiolase== | ||
| - | <StructureSection load='3goa' size='340' side='right' caption='[[3goa]], [[Resolution|resolution]] 1.70Å' scene=''> | + | <StructureSection load='3goa' size='340' side='right'caption='[[3goa]], [[Resolution|resolution]] 1.70Å' scene=''> |
== Structural highlights == | == Structural highlights == | ||
| - | <table><tr><td colspan='2'>[[3goa]] is a 2 chain structure | + | <table><tr><td colspan='2'>[[3goa]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3GOA OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3GOA FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene></td></tr> | + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene></td></tr> |
<tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene></td></tr> | <tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene></td></tr> | ||
| - | + | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/Acetyl-CoA_C-acyltransferase Acetyl-CoA C-acyltransferase], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.3.1.16 2.3.1.16] </span></td></tr> | |
| - | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[ | + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=3goa FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3goa OCA], [https://pdbe.org/3goa PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3goa RCSB], [https://www.ebi.ac.uk/pdbsum/3goa PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3goa ProSAT], [https://www.topsan.org/Proteins/CSGID/3goa TOPSAN]</span></td></tr> |
| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | + | |
</table> | </table> | ||
== Function == | == Function == | ||
| - | [[ | + | [[https://www.uniprot.org/uniprot/FADA_SALTY FADA_SALTY]] Catalyzes the final step of fatty acid oxidation in which acetyl-CoA is released and the CoA ester of a fatty acid two carbons shorter is formed. Involved in the aerobic and anaerobic degradation of long-chain fatty acids (By similarity). |
== Evolutionary Conservation == | == Evolutionary Conservation == | ||
[[Image:Consurf_key_small.gif|200px|right]] | [[Image:Consurf_key_small.gif|200px|right]] | ||
Check<jmol> | Check<jmol> | ||
<jmolCheckbox> | <jmolCheckbox> | ||
| - | <scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/go/3goa_consurf.spt"</scriptWhenChecked> | + | <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/go/3goa_consurf.spt"</scriptWhenChecked> |
<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> | <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> | ||
<text>to colour the structure by Evolutionary Conservation</text> | <text>to colour the structure by Evolutionary Conservation</text> | ||
</jmolCheckbox> | </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/ | + | </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=3goa ConSurf]. |
<div style="clear:both"></div> | <div style="clear:both"></div> | ||
==See Also== | ==See Also== | ||
| - | *[[Thiolase|Thiolase]] | + | *[[Thiolase 3D structures|Thiolase 3D structures]] |
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: Acetyl-CoA C-acyltransferase]] | [[Category: Acetyl-CoA C-acyltransferase]] | ||
| - | [[Category: | + | [[Category: Large Structures]] |
[[Category: Anderson, S M]] | [[Category: Anderson, S M]] | ||
[[Category: Anderson, W F]] | [[Category: Anderson, W F]] | ||
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[[Category: Acyltransferase]] | [[Category: Acyltransferase]] | ||
[[Category: Csgid]] | [[Category: Csgid]] | ||
| + | [[Category: Cytoplasm]] | ||
[[Category: Fatty acid]] | [[Category: Fatty acid]] | ||
[[Category: Fatty acid metabolism]] | [[Category: Fatty acid metabolism]] | ||
Current revision
Crystal structure of the Salmonella typhimurium FadA 3-ketoacyl-CoA thiolase
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Categories: Acetyl-CoA C-acyltransferase | Large Structures | Anderson, S M | Anderson, W F | Structural genomic | Onopriyenko, O | Papazisi, L | Savchenko, A | Skarina, T | Wawrzak, Z | Acyltransferase | Csgid | Cytoplasm | Fatty acid | Fatty acid metabolism | Idp01071 | Lipid degradation | Lipid metabolism | Metabolism | Phospholipid | Transferase
