2px6
From Proteopedia
(Difference between revisions)
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==Crystal structure of the thioesterase domain of human fatty acid synthase inhibited by Orlistat== | ==Crystal structure of the thioesterase domain of human fatty acid synthase inhibited by Orlistat== | ||
- | <StructureSection load='2px6' size='340' side='right' caption='[[2px6]], [[Resolution|resolution]] 2.30Å' scene=''> | + | <StructureSection load='2px6' size='340' side='right'caption='[[2px6]], [[Resolution|resolution]] 2.30Å' scene=''> |
== Structural highlights == | == Structural highlights == | ||
- | <table><tr><td colspan='2'>[[2px6]] is a 2 chain structure with sequence from [ | + | <table><tr><td colspan='2'>[[2px6]] is a 2 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=2PX6 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2PX6 FirstGlance]. <br> |
- | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=DH9:(2S,3S,5S)-5-[(N-FORMYL-L-LEUCYL)OXY]-2-HEXYL-3-HYDROXYHEXADECANOIC+ACID'>DH9</scene>, <scene name='pdbligand=DTT:2,3-DIHYDROXY-1,4-DITHIOBUTANE'>DTT</scene></td></tr> | + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=DH9:(2S,3S,5S)-5-[(N-FORMYL-L-LEUCYL)OXY]-2-HEXYL-3-HYDROXYHEXADECANOIC+ACID'>DH9</scene>, <scene name='pdbligand=DTT:2,3-DIHYDROXY-1,4-DITHIOBUTANE'>DTT</scene></td></tr> |
- | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">FAS ([ | + | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">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=2px6 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2px6 OCA], [https://pdbe.org/2px6 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2px6 RCSB], [https://www.ebi.ac.uk/pdbsum/2px6 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2px6 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]] | ||
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==See Also== | ==See Also== | ||
- | *[[Fatty acid synthase|Fatty acid synthase]] | + | *[[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: IV, C W.Pemble]] | [[Category: IV, C W.Pemble]] | ||
[[Category: Johnson, L C]] | [[Category: Johnson, L C]] |
Revision as of 15:35, 17 June 2021
Crystal structure of the thioesterase domain of human fatty acid synthase inhibited by Orlistat
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