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3hhd
From Proteopedia
(Difference between revisions)
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==Structure of the Human Fatty Acid Synthase KS-MAT Didomain as a Framework for Inhibitor Design.== | ==Structure of the Human Fatty Acid Synthase KS-MAT Didomain as a Framework for Inhibitor Design.== | ||
| - | <StructureSection load='3hhd' size='340' side='right' caption='[[3hhd]], [[Resolution|resolution]] 2.15Å' scene=''> | + | <StructureSection load='3hhd' size='340' side='right'caption='[[3hhd]], [[Resolution|resolution]] 2.15Å' scene=''> |
== Structural highlights == | == Structural highlights == | ||
| - | <table><tr><td colspan='2'>[[3hhd]] is a 4 chain structure with sequence from [ | + | <table><tr><td colspan='2'>[[3hhd]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3HHD OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3HHD FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene></td></tr> | + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene></td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">FASN, FAS ([ | + | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">FASN, FAS ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</td></tr> |
| - | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[ | + | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/Fatty-acid_synthase Fatty-acid synthase], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.3.1.85 2.3.1.85] </span></td></tr> |
| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</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=3hhd FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3hhd OCA], [https://pdbe.org/3hhd PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3hhd RCSB], [https://www.ebi.ac.uk/pdbsum/3hhd PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3hhd ProSAT]</span></td></tr> |
</table> | </table> | ||
== Function == | == 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 == | == 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/hh/3hhd_consurf.spt"</scriptWhenChecked> | + | <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/hh/3hhd_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> | ||
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</div> | </div> | ||
<div class="pdbe-citations 3hhd" style="background-color:#fffaf0;"></div> | <div class="pdbe-citations 3hhd" style="background-color:#fffaf0;"></div> | ||
| + | |||
| + | ==See Also== | ||
| + | *[[Acyl carrier protein synthase 3D structures|Acyl carrier protein synthase 3D structures]] | ||
| + | *[[Fatty acid synthase 3D structures|Fatty acid synthase 3D structures]] | ||
== References == | == References == | ||
<references/> | <references/> | ||
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[[Category: Fatty-acid synthase]] | [[Category: Fatty-acid synthase]] | ||
[[Category: Human]] | [[Category: Human]] | ||
| + | [[Category: Large Structures]] | ||
[[Category: Benz, J]] | [[Category: Benz, J]] | ||
[[Category: Pappenberger, G M]] | [[Category: Pappenberger, G M]] | ||
Revision as of 12:47, 23 March 2022
Structure of the Human Fatty Acid Synthase KS-MAT Didomain as a Framework for Inhibitor Design.
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Categories: Fatty-acid synthase | Human | Large Structures | Benz, J | Pappenberger, G M | Rudolph, M G | Thoma, R | Acetylation | Cytoplasm | Fatty acid biosynthesis | Fatty acid synthase | Fatty acid synthesis | Hydrolase | Lipid synthesis | Lyase | Megasynthase | Multienzyme | Multifunctional enzyme | Nad | Nadp | Oxidoreductase | Phosphopantetheine | Phosphoprotein | Pyridoxal phosphate | Transferase
