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2wat
From Proteopedia
(Difference between revisions)
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<StructureSection load='2wat' size='340' side='right'caption='[[2wat]], [[Resolution|resolution]] 2.20Å' scene=''> | <StructureSection load='2wat' size='340' side='right'caption='[[2wat]], [[Resolution|resolution]] 2.20Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
| - | <table><tr><td colspan='2'>[[2wat]] is a 6 chain structure with sequence from [ | + | <table><tr><td colspan='2'>[[2wat]] is a 6 chain structure with sequence from [https://en.wikipedia.org/wiki/Atcc_18824 Atcc 18824]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2WAT OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2WAT FirstGlance]. <br> |
</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>, <scene name='pdbligand=COA:COENZYME+A'>COA</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene></td></tr> | </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>, <scene name='pdbligand=COA:COENZYME+A'>COA</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene></td></tr> | ||
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[2vkz|2vkz]], [[2uv8|2uv8]], [[2was|2was]]</td></tr> | + | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[2vkz|2vkz]], [[2uv8|2uv8]], [[2was|2was]]</div></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=2wat FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2wat OCA], [https://pdbe.org/2wat PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2wat RCSB], [https://www.ebi.ac.uk/pdbsum/2wat PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2wat ProSAT]</span></td></tr> |
</table> | </table> | ||
== Function == | == Function == | ||
| - | [[ | + | [[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]] | ||
Revision as of 11:02, 6 April 2022
Structure of the fungal type I FAS PPT domain in complex with CoA
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Categories: Atcc 18824 | Large Structures | Grininger, M | Johansson, P | Koestler, C | Mulincacci, B | Coa | Fa | Fatty acid biosynthesis | Lipid synthesis | Multifunctional enzyme | Nad | Nadp | Oxidoreductase | Phosphopantetheine | Phosphopantetheine transferase | Phosphopantetheinylation | Phosphoprotein | Ppt | Transferase

