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3hhd
From Proteopedia
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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/Homo_sapiens Homo sapiens]. 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=' | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.15Å</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=' | + | <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> |
| - | <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/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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==See Also== | ==See Also== | ||
| - | *[[Acyl carrier protein synthase|Acyl carrier protein synthase]] | + | *[[Acyl carrier protein synthase 3D structures|Acyl carrier protein synthase 3D structures]] |
| - | *[[Fatty acid synthase|Fatty acid synthase]] | + | *[[Fatty acid synthase 3D structures|Fatty acid synthase 3D structures]] |
== References == | == References == | ||
<references/> | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
| - | [[Category: | + | [[Category: Homo sapiens]] |
| - | [[Category: | + | [[Category: Large Structures]] |
| - | [[Category: Benz | + | [[Category: Benz J]] |
| - | [[Category: Pappenberger | + | [[Category: Pappenberger GM]] |
| - | [[Category: Rudolph | + | [[Category: Rudolph MG]] |
| - | [[Category: Thoma | + | [[Category: Thoma R]] |
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Current revision
Structure of the Human Fatty Acid Synthase KS-MAT Didomain as a Framework for Inhibitor Design.
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