2px6: 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]] 2.30&Aring;' scene=''>
<StructureSection load='2px6' size='340' side='right'caption='[[2px6]], [[Resolution|resolution]] 2.30&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[2px6]] is a 2 chain structure with sequence from [http://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 [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2PX6 FirstGlance]. <br>
<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 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</td></tr>
<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'>[http://en.wikipedia.org/wiki/Fatty-acid_synthase Fatty-acid synthase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.3.1.85 2.3.1.85] </span></td></tr>
<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'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2px6 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2px6 OCA], [http://pdbe.org/2px6 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2px6 RCSB], [http://www.ebi.ac.uk/pdbsum/2px6 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2px6 ProSAT]</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=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 ==
[[http://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.  
[[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]]