2uv8

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<tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=GVL:O-[(R)-{[(3R)-4-AMINO-3-HYDROXY-2,2-DIMETHYL-4-OXOBUTYL]OXY}(HYDROXY)PHOSPHORYL]-L-SERINE'>GVL</scene></td></tr>
<tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=GVL:O-[(R)-{[(3R)-4-AMINO-3-HYDROXY-2,2-DIMETHYL-4-OXOBUTYL]OXY}(HYDROXY)PHOSPHORYL]-L-SERINE'>GVL</scene></td></tr>
<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Fatty-acyl-CoA_synthase Fatty-acyl-CoA synthase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.3.1.86 2.3.1.86] </span></td></tr>
<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Fatty-acyl-CoA_synthase Fatty-acyl-CoA synthase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.3.1.86 2.3.1.86] </span></td></tr>
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<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=2uv8 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2uv8 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2uv8 RCSB], [http://www.ebi.ac.uk/pdbsum/2uv8 PDBsum]</span></td></tr>
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<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=2uv8 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2uv8 OCA], [http://pdbe.org/2uv8 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2uv8 RCSB], [http://www.ebi.ac.uk/pdbsum/2uv8 PDBsum]</span></td></tr>
</table>
</table>
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{{Large structure}}
== Function ==
== Function ==
[[http://www.uniprot.org/uniprot/FAS2_YEAST FAS2_YEAST]] Fatty acid synthetase catalyzes the formation of long-chain fatty acids from acetyl-CoA, malonyl-CoA and NADPH. The alpha subunit contains domains for: acyl carrier protein, 3-oxoacyl-[acyl-carrier-protein] reductase, and 3-oxoacyl-[acyl-carrier-protein] synthase. This subunit coordinates the binding of the six beta subunits to the enzyme complex.[HAMAP-Rule:MF_00101] [[http://www.uniprot.org/uniprot/FAS1_YEAST FAS1_YEAST]] Fatty acid synthetase catalyzes the formation of long-chain fatty acids from acetyl-CoA, malonyl-CoA and NADPH. The beta subunit contains domains for: [acyl-carrier-protein] acetyltransferase and malonyltransferase, S-acyl fatty acid synthase thioesterase, enoyl-[acyl-carrier-protein] reductase, and 3-hydroxypalmitoyl-[acyl-carrier-protein] dehydratase.
[[http://www.uniprot.org/uniprot/FAS2_YEAST FAS2_YEAST]] Fatty acid synthetase catalyzes the formation of long-chain fatty acids from acetyl-CoA, malonyl-CoA and NADPH. The alpha subunit contains domains for: acyl carrier protein, 3-oxoacyl-[acyl-carrier-protein] reductase, and 3-oxoacyl-[acyl-carrier-protein] synthase. This subunit coordinates the binding of the six beta subunits to the enzyme complex.[HAMAP-Rule:MF_00101] [[http://www.uniprot.org/uniprot/FAS1_YEAST FAS1_YEAST]] Fatty acid synthetase catalyzes the formation of long-chain fatty acids from acetyl-CoA, malonyl-CoA and NADPH. The beta subunit contains domains for: [acyl-carrier-protein] acetyltransferase and malonyltransferase, S-acyl fatty acid synthase thioesterase, enoyl-[acyl-carrier-protein] reductase, and 3-hydroxypalmitoyl-[acyl-carrier-protein] dehydratase.
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<text>to colour the structure by Evolutionary Conservation</text>
<text>to colour the structure by Evolutionary Conservation</text>
</jmolCheckbox>
</jmolCheckbox>
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</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/chain_selection.php?pdb_ID=2ata ConSurf].
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</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=2uv8 ConSurf].
<div style="clear:both"></div>
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
<div style="background-color:#fffaf0;">
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
</div>
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<div class="pdbe-citations 2uv8" style="background-color:#fffaf0;"></div>
==See Also==
==See Also==

Revision as of 15:59, 9 February 2016

CRYSTAL STRUCTURE OF YEAST FATTY ACID SYNTHASE WITH STALLED ACYL CARRIER PROTEIN AT 3.1 ANGSTROM RESOLUTION

2uv8, resolution 3.10Å

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