1cwu: Difference between revisions

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[[Image:1cwu.png|left|200px]]


{{STRUCTURE_1cwu|  PDB=1cwu  |  SCENE=  }}
==BRASSICA NAPUS ENOYL ACP REDUCTASE A138G MUTANT COMPLEXED WITH NAD+ AND THIENODIAZABORINE==
 
<StructureSection load='1cwu' size='340' side='right'caption='[[1cwu]], [[Resolution|resolution]] 2.50&Aring;' scene=''>
===BRASSICA NAPUS ENOYL ACP REDUCTASE A138G MUTANT COMPLEXED WITH NAD+ AND THIENODIAZABORINE===
== Structural highlights ==
 
<table><tr><td colspan='2'>[[1cwu]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Brassica_napus Brassica napus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1CWU OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1CWU FirstGlance]. <br>
{{ABSTRACT_PUBMED_10521472}}
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.5&#8491;</td></tr>
 
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=NAD:NICOTINAMIDE-ADENINE-DINUCLEOTIDE'>NAD</scene>, <scene name='pdbligand=TDB:6-METHYL-2(PROPANE-1-SULFONYL)-2H-THIENO[3,2-D][1,2,3]DIAZABORININ-1-OL'>TDB</scene></td></tr>
==About this Structure==
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1cwu FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1cwu OCA], [https://pdbe.org/1cwu PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1cwu RCSB], [https://www.ebi.ac.uk/pdbsum/1cwu PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1cwu ProSAT]</span></td></tr>
[[1cwu]] is a 2 chain structure of [[Enoyl-Acyl-Carrier Protein Reductase]] with sequence from [http://en.wikipedia.org/wiki/Brassica_napus Brassica napus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1CWU OCA].  
</table>
== Function ==
[https://www.uniprot.org/uniprot/FABI_BRANA FABI_BRANA] Catalyzes the NAD-dependent reduction of a carbon-carbon double bond in an enoyl moiety that is covalently linked to an acyl carrier protein (ACP). Catalyzes the last reduction step in the de novo synthesis cycle of fatty acids. Involved in the elongation cycle of fatty acids which are used in lipid metabolism. Required for normal plant growth (By similarity).
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
Check<jmol>
  <jmolCheckbox>
    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/cw/1cwu_consurf.spt"</scriptWhenChecked>
    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
    <text>to colour the structure by Evolutionary Conservation</text>
  </jmolCheckbox>
</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=1cwu ConSurf].
<div style="clear:both"></div>


==See Also==
==See Also==
*[[Enoyl-Acyl-Carrier Protein Reductase|Enoyl-Acyl-Carrier Protein Reductase]]
*[[Enoyl-Acyl-Carrier Protein Reductase 3D structures|Enoyl-Acyl-Carrier Protein Reductase 3D structures]]
 
__TOC__
==Reference==
</StructureSection>
<ref group="xtra">PMID:010521472</ref><references group="xtra"/>
[[Category: Brassica napus]]
[[Category: Brassica napus]]
[[Category: Rafferty, J B.]]
[[Category: Large Structures]]
[[Category: Rice, D W.]]
[[Category: Rafferty JB]]
[[Category: Roujeinikova, A.]]
[[Category: Rice DW]]
[[Category: Diazaborine]]
[[Category: Roujeinikova A]]
[[Category: Oxidoreductase]]
[[Category: Plant lipid biosynthesis]]

Latest revision as of 06:46, 7 February 2024

BRASSICA NAPUS ENOYL ACP REDUCTASE A138G MUTANT COMPLEXED WITH NAD+ AND THIENODIAZABORINE

1cwu, resolution 2.50Å

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