2uv8

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Current revision (14:55, 13 December 2023) (edit) (undo)
 
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== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[2uv8]] is a 6 chain structure with sequence from [https://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2UV8 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2UV8 FirstGlance]. <br>
<table><tr><td colspan='2'>[[2uv8]] is a 6 chain structure with sequence from [https://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2UV8 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2UV8 FirstGlance]. <br>
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</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=FMN:FLAVIN+MONONUCLEOTIDE'>FMN</scene></td></tr>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 3.1&#8491;</td></tr>
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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>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=FMN:FLAVIN+MONONUCLEOTIDE'>FMN</scene>, <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>
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<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/Fatty-acyl-CoA_synthase Fatty-acyl-CoA synthase], with EC number [https://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'>[https://proteopedia.org/fgij/fg.htm?mol=2uv8 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2uv8 OCA], [https://pdbe.org/2uv8 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2uv8 RCSB], [https://www.ebi.ac.uk/pdbsum/2uv8 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2uv8 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=2uv8 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2uv8 OCA], [https://pdbe.org/2uv8 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2uv8 RCSB], [https://www.ebi.ac.uk/pdbsum/2uv8 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2uv8 ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
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[[https://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] [[https://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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[https://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]
== Evolutionary Conservation ==
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
[[Image:Consurf_key_small.gif|200px|right]]
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__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: Fatty-acyl-CoA synthase]]
 
[[Category: Large Structures]]
[[Category: Large Structures]]
[[Category: Saccharomyces cerevisiae]]
[[Category: Saccharomyces cerevisiae]]
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[[Category: Ban, N]]
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[[Category: Ban N]]
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[[Category: Frick, C]]
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[[Category: Frick C]]
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[[Category: Jenni, S]]
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[[Category: Jenni S]]
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[[Category: Leibundgut, M]]
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[[Category: Leibundgut M]]
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[[Category: Acetyl transferase]]
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[[Category: Acyl carrier protein]]
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[[Category: Dehydratase]]
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[[Category: Enoyl reductase]]
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[[Category: Fatty acid biosynthesis]]
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[[Category: Fatty acid synthase]]
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[[Category: Fatty acid synthesis]]
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[[Category: Hydrolase]]
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[[Category: Ketoacyl reductase]]
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[[Category: Ketoacyl synthase]]
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[[Category: Lipid synthesis]]
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[[Category: Lyase]]
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[[Category: Malonyl/palmitoyl transferase]]
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[[Category: Multifunctional enzyme]]
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[[Category: Nad]]
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[[Category: Nadp]]
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[[Category: Oxidoreductase]]
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[[Category: Phosphopantetheine]]
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[[Category: Phosphorylation]]
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[[Category: Substrate shuttling]]
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[[Category: Transferase]]
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[[Category: Yeast]]
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Current revision

Crystal structure of yeast fatty acid synthase with stalled acyl carrier protein at 3.1 angstrom resolution

PDB ID 2uv8

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