
<?xml version="1.0"?>
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	<id>https://proteopedia.org/api.php?action=feedcontributions&amp;feedformat=atom&amp;user=Appoline+Dubois</id>
	<title>Proteopedia - User contributions [en]</title>
	<link rel="self" type="application/atom+xml" href="https://proteopedia.org/api.php?action=feedcontributions&amp;feedformat=atom&amp;user=Appoline+Dubois"/>
	<link rel="alternate" type="text/html" href="https://proteopedia.org/Special:Contributions/Appoline_Dubois"/>
	<updated>2026-10-05T15:59:18Z</updated>
	<subtitle>User contributions</subtitle>
	<generator>MediaWiki 1.43.8</generator>
	<entry>
		<id>https://proteopedia.org/index.php?title=Sandbox_Reserved_1108&amp;diff=3144211</id>
		<title>Sandbox Reserved 1108</title>
		<link rel="alternate" type="text/html" href="https://proteopedia.org/index.php?title=Sandbox_Reserved_1108&amp;diff=3144211"/>
		<updated>2020-01-17T16:41:47Z</updated>

		<summary type="html">&lt;p&gt;Appoline Dubois: &lt;/p&gt;
&lt;hr /&gt;
&lt;div&gt;{{Sandbox_ESBS_2019}}&amp;lt;!-- PLEASE ADD YOUR CONTENT BELOW HERE --&amp;gt;&lt;br /&gt;
==4iv6==&lt;br /&gt;
&amp;lt;StructureSection load=&#039;1stp&#039; size=&#039;340&#039; side=&#039;right&#039; caption=&#039;Caption for this structure&#039; scene=&#039;&#039;&amp;gt;&lt;br /&gt;
4iv6 is an  enzyme &#039;&#039;Mycobacterium tuberculosis&#039;&#039; which get his structure analyzed by Baugh et al. [https://www.ncbi.nlm.nih.gov/pubmed/25613812] with other enzymes homologue in order to fight &#039;&#039;Mycobacterium tuberculosis&#039;&#039; relative infections.&lt;br /&gt;
&lt;br /&gt;
== Function ==&lt;br /&gt;
4iv6 functions were not studied and only structural infos are disponible.&lt;br /&gt;
Nevertheless we can consider datas from other E.C.1.3.8.1[https://enzyme.expasy.org/EC/1.3.8.1] which came from other organisms.&lt;br /&gt;
E.C.1.3.8.1[https://enzyme.expasy.org/EC/1.3.8.1] is communly found in following pathways with various functions:&lt;br /&gt;
&lt;br /&gt;
[[Analine metabolism]]:[https://www.brenda-enzymes.info/pathway_index.php?pathway=alanine%20metabolism&amp;amp;ecno=1.3.8.1]&lt;br /&gt;
&lt;br /&gt;
[[Butanoate metabolism]]:[https://www.genome.jp/kegg-bin/show_pathway?map00650+1.3.8.1]&lt;br /&gt;
&lt;br /&gt;
[[Lipids metabolism]] : [https://www.brenda-enzymes.info/pathway_index.php?pathway=lipid%20metabolism&amp;amp;ecno=1.3.8.1][https://www.genome.jp/kegg-bin/show_pathway?map00071+1.3.8.1]&lt;br /&gt;
&lt;br /&gt;
[[Valine Leucine and isoleucine pathways]]:[https://www.genome.jp/kegg-bin/show_pathway?map00280+1.3.8.1]&lt;br /&gt;
&lt;br /&gt;
&lt;br /&gt;
==Primary and Secondary structure&amp;lt;ref&amp;gt;http://www.rcsb.org/structure/4IV6&amp;lt;/ref&amp;gt;==&lt;br /&gt;
&lt;br /&gt;
Isovaleryl-CoA dehydrogenase is the assembly of &#039;&#039;&#039;&amp;lt;scene name=&#039;82/829361/2asymunit/1&#039;&amp;gt;two asymmetric units&amp;lt;/scene&amp;gt;&#039;&#039;&#039; each composed of &#039;&#039;&#039;two chains &amp;lt;scene name=&#039;82/829361/Chainea_asymunit/2&#039;&amp;gt;A&amp;lt;/scene&amp;gt; and &amp;lt;scene name=&#039;82/829361/Chaineb_asymunit/1&#039;&amp;gt;B&amp;lt;/scene&amp;gt;&#039;&#039;&#039;. Each of the two chains A and B are composed of 388 amino acids. An asymmetric unit is therefore composed of 776 amino acids and has a molecular weight of 86233.70 Da.&lt;br /&gt;
1% of the unit&#039;s amino acid have incomplete sidechains, which means that there are 11 missing residue in the assymetric unit.&amp;lt;ref&amp;gt;https://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4iv6&amp;lt;/ref&amp;gt;&lt;br /&gt;
&lt;br /&gt;
The A chain is made up of &amp;lt;scene name=&#039;82/829361/Helixalphachaina_asymunit/1&#039;&amp;gt;17 helices&amp;lt;/scene&amp;gt; (involving 221 residues) and &amp;lt;scene name=&#039;82/829361/Betasheetchaina_asymunit/1&#039;&amp;gt;14 beta-sheets&amp;lt;/scene&amp;gt; (61 residues).&lt;br /&gt;
Chain B is formed of &amp;lt;scene name=&#039;82/829361/Helixchainb_asymunit/1&#039;&amp;gt;17 helices&amp;lt;/scene&amp;gt; (involving 218 residues) and &amp;lt;scene name=&#039;82/829361/Betasheetchainb_asymunit/1&#039;&amp;gt;14 beta-sheets&amp;lt;/scene&amp;gt; (62 residues). &lt;br /&gt;
&lt;br /&gt;
==Tertiary structures==&lt;br /&gt;
&lt;br /&gt;
The two chains A and B of the isovaleryl-CoA dehydrogenase are linked by a &amp;lt;scene name=&#039;82/829361/Ligand_asymunit/1&#039;&amp;gt;ligand&amp;lt;/scene&amp;gt; (Dihydroflavine-Adenine Dinucleotide also known as [https://pubchem.ncbi.nlm.nih.gov/compound/Dihydroflavine-adenine-dinucleotide FADH2] ).&lt;br /&gt;
&lt;br /&gt;
The protein is a tetramer, the surface between the two monomers of a single dimer of an acyl-CoA dehydrogenase contains the FAD binding sites and has extensive bonding interactions. There are 2 active sites in the tetramer, each of these 2 sites contains a FAD molecule and an acyl-CoA substrate binding site. &amp;lt;ref&amp;gt;https://en.wikipedia.org/wiki/Flavin_adenine_dinucleotide&amp;lt;/ref&amp;gt;&lt;br /&gt;
&lt;br /&gt;
==Enzymatic reaction&amp;lt;ref&amp;gt;http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl?pdbcode=4iv6&amp;lt;/ref&amp;gt;&amp;lt;ref&amp;gt;https://www.ebi.ac.uk/intenz/query?cmd=SearchEC&amp;amp;ec=1.3.8.1&amp;lt;/ref&amp;gt;&amp;lt;ref&amp;gt;https://enzyme.expasy.org/EC/1.3.8.1&amp;lt;/ref&amp;gt;==&lt;br /&gt;
&lt;br /&gt;
[[Enzyme accepted name]]: Short-chain acyl-CoA dehydrogenase&lt;br /&gt;
&lt;br /&gt;
[[Other names]]:Butanoyl-CoA dehydrogenase, Butyryl dehydrogenase, Short-chain acyl CoA dehydrogenase, Unsatured acyl-CoA reductase.&lt;br /&gt;
&lt;br /&gt;
[[Enzyme class]]: E.C.1.3.8.1[https://enzyme.expasy.org/EC/1.3.8.1]&lt;br /&gt;
&lt;br /&gt;
[[Substrate]]: A short-chain acyl CoA &lt;br /&gt;
&lt;br /&gt;
[[Prosthetic group]]: 1 electron-transfer flavoprotein such as FDA, for every Subunits &lt;br /&gt;
&lt;br /&gt;
[[Products]]: a short-chain trans-2,3-dehydroacyl-CoA + reduced electron-transfer flavoprotein&lt;br /&gt;
&lt;br /&gt;
[[Informed Pathways]]: Fatty acid degradation&lt;br /&gt;
&lt;br /&gt;
[[Other information]]:&lt;br /&gt;
&lt;br /&gt;
The enzyme from beef liver can accept acyl-chain lengths from 3 to 8 carbon atoms. From different organism the range can vary so we ignore if &#039;&#039;Mycobacterium tuberculosis&#039;&#039; gets the same lengths resolution.&lt;br /&gt;
&lt;br /&gt;
The highest activity reported for beef liver enzyme was for substrates with 4 and 5 carbon acyl-chain lengths.&lt;br /&gt;
&lt;br /&gt;
==4IV6 as a research tool==&lt;br /&gt;
&lt;br /&gt;
4iv6 which belong to &#039;&#039;Mycobacterium tuberculosis&#039;&#039; was studied with other protein homolog.&lt;br /&gt;
They were chosen to be studied as potential TB-Drugs target&lt;br /&gt;
Studies have been made on homolog similarities aimed on their active site because with the knowledges of many homolog active site structure and how they work, we can design a inhibitor of those enzyme which can stop essential reaction and reduce or stop &#039;&#039;Mycobacterium tuberculosis&#039;&#039; infection.&lt;br /&gt;
This strategy is called an « Homolog-rescue strategy ».&lt;br /&gt;
This strategy can be generalized for other drug target for other diseases.&lt;br /&gt;
&lt;br /&gt;
&lt;br /&gt;
== Structural highlights summary ==&lt;br /&gt;
&lt;br /&gt;
&amp;lt;scene name=&#039;82/829361/Biological_unit/1&#039;&amp;gt;Biological unit&amp;lt;/scene&amp;gt;&lt;br /&gt;
&lt;br /&gt;
&amp;lt;scene name=&#039;82/829361/2asymunit/1&#039;&amp;gt;Asymmetric units&amp;lt;/scene&amp;gt;&lt;br /&gt;
&lt;br /&gt;
&amp;lt;scene name=&#039;82/829361/Betasheetchaina_asymunit/1&#039;&amp;gt;Beta-sheets&amp;lt;/scene&amp;gt;&lt;br /&gt;
&lt;br /&gt;
&amp;lt;scene name=&#039;82/829361/Helixalphachaina_asymunit/1&#039;&amp;gt;Helices&amp;lt;/scene&amp;gt;&lt;br /&gt;
&lt;br /&gt;
&amp;lt;scene name=&#039;82/829361/Secondary_structure/1&#039;&amp;gt;Secondary structure&amp;lt;/scene&amp;gt;  &lt;br /&gt;
&lt;br /&gt;
&amp;lt;scene name=&#039;82/829361/Chainea_asymunit/2&#039;&amp;gt;A chain&amp;lt;/scene&amp;gt; &lt;br /&gt;
&lt;br /&gt;
&amp;lt;scene name=&#039;82/829361/Chaineb_asymunit/1&#039;&amp;gt;B chain&amp;lt;/scene&amp;gt;&lt;br /&gt;
&lt;br /&gt;
&amp;lt;scene name=&#039;82/829361/Hydrophobic/1&#039;&amp;gt;Hydrophobic region&amp;lt;/scene&amp;gt;&lt;br /&gt;
&lt;br /&gt;
&amp;lt;/StructureSection&amp;gt;&lt;br /&gt;
== References ==&lt;br /&gt;
&amp;lt;references/&amp;gt;&lt;/div&gt;</summary>
		<author><name>Appoline Dubois</name></author>
	</entry>
	<entry>
		<id>https://proteopedia.org/index.php?title=Sandbox_Reserved_1108&amp;diff=3144209</id>
		<title>Sandbox Reserved 1108</title>
		<link rel="alternate" type="text/html" href="https://proteopedia.org/index.php?title=Sandbox_Reserved_1108&amp;diff=3144209"/>
		<updated>2020-01-17T16:33:14Z</updated>

		<summary type="html">&lt;p&gt;Appoline Dubois: &lt;/p&gt;
&lt;hr /&gt;
&lt;div&gt;{{Sandbox_ESBS_2019}}&amp;lt;!-- PLEASE ADD YOUR CONTENT BELOW HERE --&amp;gt;&lt;br /&gt;
==4iv6==&lt;br /&gt;
&amp;lt;StructureSection load=&#039;1stp&#039; size=&#039;340&#039; side=&#039;right&#039; caption=&#039;Caption for this structure&#039; scene=&#039;&#039;&amp;gt;&lt;br /&gt;
4iv6 is an  enzyme &#039;&#039;Mycobacterium tuberculosis&#039;&#039; which get his structure analyzed by Baugh et al. [https://www.ncbi.nlm.nih.gov/pubmed/25613812] with other enzymes homologue in order to fight &#039;&#039;Mycobacterium tuberculosis&#039;&#039; relative infections.&lt;br /&gt;
&lt;br /&gt;
== Function ==&lt;br /&gt;
4iv6 functions were not studied and only structural infos are disponible.&lt;br /&gt;
Nevertheless we can consider datas from other E.C.1.3.8.1[https://enzyme.expasy.org/EC/1.3.8.1] which came from other organisms.&lt;br /&gt;
E.C.1.3.8.1[https://enzyme.expasy.org/EC/1.3.8.1] is communly found in following pathways with various functions:&lt;br /&gt;
&lt;br /&gt;
[[Analine metabolism]]:[https://www.brenda-enzymes.info/pathway_index.php?pathway=alanine%20metabolism&amp;amp;ecno=1.3.8.1]&lt;br /&gt;
&lt;br /&gt;
[[Butanoate metabolism]]:[https://www.genome.jp/kegg-bin/show_pathway?map00650+1.3.8.1]&lt;br /&gt;
&lt;br /&gt;
[[Lipids metabolism]] : [https://www.brenda-enzymes.info/pathway_index.php?pathway=lipid%20metabolism&amp;amp;ecno=1.3.8.1][https://www.genome.jp/kegg-bin/show_pathway?map00071+1.3.8.1]&lt;br /&gt;
&lt;br /&gt;
[[Valine Leucine and isoleucine pathways]]:[https://www.genome.jp/kegg-bin/show_pathway?map00280+1.3.8.1]&lt;br /&gt;
&lt;br /&gt;
&lt;br /&gt;
==Primary and Secondary structure&amp;lt;ref&amp;gt;http://www.rcsb.org/structure/4IV6&amp;lt;/ref&amp;gt;==&lt;br /&gt;
&lt;br /&gt;
Isovaleryl-CoA dehydrogenase is the assembly of &#039;&#039;&#039;&amp;lt;scene name=&#039;82/829361/2asymunit/1&#039;&amp;gt;two asymmetric units&amp;lt;/scene&amp;gt;&#039;&#039;&#039; each composed of &#039;&#039;&#039;two chains &amp;lt;scene name=&#039;82/829361/Chainea_asymunit/2&#039;&amp;gt;A&amp;lt;/scene&amp;gt; and &amp;lt;scene name=&#039;82/829361/Chaineb_asymunit/1&#039;&amp;gt;B&amp;lt;/scene&amp;gt;&#039;&#039;&#039;. Each of the two chains A and B are composed of 388 amino acids. An asymmetric unit is therefore composed of 776 amino acids and has a molecular weight of 86233.70 Da.&lt;br /&gt;
1% of the unit&#039;s amino acid have incomplete sidechains, which means that there are 11 missing residue in the assymetric unit.&amp;lt;ref&amp;gt;https://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4iv6&amp;lt;/ref&amp;gt;&lt;br /&gt;
&lt;br /&gt;
The A chain is made up of &amp;lt;scene name=&#039;82/829361/Helixalphachaina_asymunit/1&#039;&amp;gt;17 helices&amp;lt;/scene&amp;gt; (involving 221 residues) and &amp;lt;scene name=&#039;82/829361/Betasheetchaina_asymunit/1&#039;&amp;gt;14 beta-sheets&amp;lt;/scene&amp;gt; (61 residues).&lt;br /&gt;
Chain B is formed of &amp;lt;scene name=&#039;82/829361/Helixchainb_asymunit/1&#039;&amp;gt;17 helices&amp;lt;/scene&amp;gt; (involving 218 residues) and &amp;lt;scene name=&#039;82/829361/Betasheetchainb_asymunit/1&#039;&amp;gt;14 beta-sheets&amp;lt;/scene&amp;gt; (62 residues). &lt;br /&gt;
&lt;br /&gt;
&lt;br /&gt;
==Tertiary structures==&lt;br /&gt;
&lt;br /&gt;
The two chains A and B of the isovaleryl-CoA dehydrogenase are linked by a &amp;lt;scene name=&#039;82/829361/Ligand_asymunit/1&#039;&amp;gt;ligand&amp;lt;/scene&amp;gt; (Dihydroflavine-Adenine Dinucleotide also known as [https://pubchem.ncbi.nlm.nih.gov/compound/Dihydroflavine-adenine-dinucleotide FADH2] ).&lt;br /&gt;
&lt;br /&gt;
The protein is a tetramer, the surface between the two monomers of a single dimer of an acyl-CoA dehydrogenase contains the FAD binding sites and has extensive bonding interactions. There are 2 active sites in the tetramer, each of these 2 sites contains a FAD molecule and an acyl-CoA substrate binding site. &amp;lt;ref&amp;gt;https://en.wikipedia.org/wiki/Flavin_adenine_dinucleotide&amp;lt;/ref&amp;gt;&lt;br /&gt;
&lt;br /&gt;
==Enzymatic reaction&amp;lt;ref&amp;gt;http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl?pdbcode=4iv6&amp;lt;/ref&amp;gt;&amp;lt;ref&amp;gt;https://www.ebi.ac.uk/intenz/query?cmd=SearchEC&amp;amp;ec=1.3.8.1&amp;lt;/ref&amp;gt;&amp;lt;ref&amp;gt;https://enzyme.expasy.org/EC/1.3.8.1&amp;lt;/ref&amp;gt;==&lt;br /&gt;
&lt;br /&gt;
[[Enzyme accepted name]]: Short-chain acyl-CoA dehydrogenase&lt;br /&gt;
&lt;br /&gt;
[[Other names]]:Butanoyl-CoA dehydrogenase, Butyryl dehydrogenase, Short-chain acyl CoA dehydrogenase, Unsatured acyl-CoA reductase.&lt;br /&gt;
&lt;br /&gt;
[[Enzyme class]]: E.C.1.3.8.1[https://enzyme.expasy.org/EC/1.3.8.1]&lt;br /&gt;
&lt;br /&gt;
[[Substrate]]: A short-chain acyl CoA &lt;br /&gt;
&lt;br /&gt;
[[Prosthetic group]]: 1 electron-transfer flavoprotein such as FDA, for every Subunits &lt;br /&gt;
&lt;br /&gt;
[[Products]]: a short-chain trans-2,3-dehydroacyl-CoA + reduced electron-transfer flavoprotein&lt;br /&gt;
&lt;br /&gt;
[[Informed Pathways]]: Fatty acid degradation&lt;br /&gt;
&lt;br /&gt;
[[Other information]]:&lt;br /&gt;
&lt;br /&gt;
The enzyme from beef liver can accept acyl-chain lengths from 3 to 8 carbon atoms. From different organism the range can vary so we ignore if &#039;&#039;Mycobacterium tuberculosis&#039;&#039; gets the same lengths resolution.&lt;br /&gt;
&lt;br /&gt;
The highest activity reported for beef liver enzyme was for substrates with 4 and 5 carbon acyl-chain lengths.&lt;br /&gt;
&lt;br /&gt;
==4IV6 as a research tool==&lt;br /&gt;
&lt;br /&gt;
4iv6 which belong to &#039;&#039;Mycobacterium tuberculosis&#039;&#039; was studied with other protein homolog.&lt;br /&gt;
They were chosen to be studied as potential TB-Drugs target&lt;br /&gt;
Studies have been made on homolog similarities aimed on their active site because with the knowledges of many homolog active site structure and how they work, we can design a inhibitor of those enzyme which can stop essential reaction and reduce or stop &#039;&#039;Mycobacterium tuberculosis&#039;&#039; infection.&lt;br /&gt;
This strategy is called an « Homolog-rescue strategy ».&lt;br /&gt;
This strategy can be generalized for other drug target for other diseases.&lt;br /&gt;
&lt;br /&gt;
&lt;br /&gt;
== Structural highlights summary ==&lt;br /&gt;
&lt;br /&gt;
&amp;lt;scene name=&#039;82/829361/Biological_unit/1&#039;&amp;gt;Biological unit&amp;lt;/scene&amp;gt;&lt;br /&gt;
&lt;br /&gt;
&amp;lt;scene name=&#039;82/829361/2asymunit/1&#039;&amp;gt;Asymmetric units&amp;lt;/scene&amp;gt;&lt;br /&gt;
&lt;br /&gt;
&amp;lt;scene name=&#039;82/829361/Betasheetchaina_asymunit/1&#039;&amp;gt;Beta-sheets&amp;lt;/scene&amp;gt;&lt;br /&gt;
&lt;br /&gt;
&amp;lt;scene name=&#039;82/829361/Helixalphachaina_asymunit/1&#039;&amp;gt;Helices&amp;lt;/scene&amp;gt;&lt;br /&gt;
&lt;br /&gt;
&amp;lt;scene name=&#039;82/829361/Secondary_structure/1&#039;&amp;gt;Secondary structure&amp;lt;/scene&amp;gt;  &lt;br /&gt;
&lt;br /&gt;
&amp;lt;scene name=&#039;82/829361/Chainea_asymunit/2&#039;&amp;gt;A chain&amp;lt;/scene&amp;gt; &lt;br /&gt;
&lt;br /&gt;
&amp;lt;scene name=&#039;82/829361/Chaineb_asymunit/1&#039;&amp;gt;B chain&amp;lt;/scene&amp;gt;&lt;br /&gt;
&lt;br /&gt;
&amp;lt;scene name=&#039;82/829361/Hydrophobic/1&#039;&amp;gt;Hydrophobic region&amp;lt;/scene&amp;gt;&lt;br /&gt;
&lt;br /&gt;
&amp;lt;/StructureSection&amp;gt;&lt;br /&gt;
== References ==&lt;br /&gt;
&amp;lt;references/&amp;gt;&lt;/div&gt;</summary>
		<author><name>Appoline Dubois</name></author>
	</entry>
	<entry>
		<id>https://proteopedia.org/index.php?title=Sandbox_Reserved_1108&amp;diff=3144208</id>
		<title>Sandbox Reserved 1108</title>
		<link rel="alternate" type="text/html" href="https://proteopedia.org/index.php?title=Sandbox_Reserved_1108&amp;diff=3144208"/>
		<updated>2020-01-17T16:21:49Z</updated>

		<summary type="html">&lt;p&gt;Appoline Dubois: &lt;/p&gt;
&lt;hr /&gt;
&lt;div&gt;{{Sandbox_ESBS_2019}}&amp;lt;!-- PLEASE ADD YOUR CONTENT BELOW HERE --&amp;gt;&lt;br /&gt;
==4iv6==&lt;br /&gt;
&amp;lt;StructureSection load=&#039;1stp&#039; size=&#039;340&#039; side=&#039;right&#039; caption=&#039;Caption for this structure&#039; scene=&#039;&#039;&amp;gt;&lt;br /&gt;
4iv6 is an  enzyme &#039;&#039;Mycobacterium tuberculosis&#039;&#039; which get his structure analyzed by Baugh et al. [https://www.ncbi.nlm.nih.gov/pubmed/25613812] with other enzymes homologue in order to fight &#039;&#039;Mycobacterium tuberculosis&#039;&#039; relative infections.&lt;br /&gt;
&lt;br /&gt;
== Function ==&lt;br /&gt;
4iv6 functions were not studied and only structural infos are disponible.&lt;br /&gt;
Nevertheless we can consider datas from other E.C.1.3.8.1[https://enzyme.expasy.org/EC/1.3.8.1] which came from other organisms.&lt;br /&gt;
E.C.1.3.8.1[https://enzyme.expasy.org/EC/1.3.8.1] is communly found in following pathways with various functions:&lt;br /&gt;
&lt;br /&gt;
[[Analine metabolism]]:[https://www.brenda-enzymes.info/pathway_index.php?pathway=alanine%20metabolism&amp;amp;ecno=1.3.8.1]&lt;br /&gt;
&lt;br /&gt;
[[Butanoate metabolism]]:[https://www.genome.jp/kegg-bin/show_pathway?map00650+1.3.8.1]&lt;br /&gt;
&lt;br /&gt;
[[Lipids metabolism]] : [https://www.brenda-enzymes.info/pathway_index.php?pathway=lipid%20metabolism&amp;amp;ecno=1.3.8.1][https://www.genome.jp/kegg-bin/show_pathway?map00071+1.3.8.1]&lt;br /&gt;
&lt;br /&gt;
[[Valine Leucine and isoleucine pathways]]:[https://www.genome.jp/kegg-bin/show_pathway?map00280+1.3.8.1]&lt;br /&gt;
&lt;br /&gt;
&lt;br /&gt;
==Primary and Secondary structure&amp;lt;ref&amp;gt;http://www.rcsb.org/structure/4IV6&amp;lt;/ref&amp;gt;==&lt;br /&gt;
&lt;br /&gt;
Isovaleryl-CoA dehydrogenase is the assembly of &#039;&#039;&#039;&amp;lt;scene name=&#039;82/829361/2asymunit/1&#039;&amp;gt;two asymmetric units&amp;lt;/scene&amp;gt;&#039;&#039;&#039; each composed of &#039;&#039;&#039;two chains &amp;lt;scene name=&#039;82/829361/Chainea_asymunit/2&#039;&amp;gt;A&amp;lt;/scene&amp;gt; and &amp;lt;scene name=&#039;82/829361/Chaineb_asymunit/1&#039;&amp;gt;B&amp;lt;/scene&amp;gt;&#039;&#039;&#039; linked by a &amp;lt;scene name=&#039;82/829361/Ligand_asymunit/1&#039;&amp;gt;ligand&amp;lt;/scene&amp;gt; (Dihydroflavine-Adenine Dinucleotide also known as [https://pubchem.ncbi.nlm.nih.gov/compound/Dihydroflavine-adenine-dinucleotide FADH2] ). Each of the two chains A and B are composed of 388 amino acids. An asymmetric unit is therefore composed of 776 amino acids and has a molecular weight of 86233.70 Da.&lt;br /&gt;
&lt;br /&gt;
The A chain is made up of &amp;lt;scene name=&#039;82/829361/Helixalphachaina_asymunit/1&#039;&amp;gt;17 helices&amp;lt;/scene&amp;gt; (involving 221 residues) and &amp;lt;scene name=&#039;82/829361/Betasheetchaina_asymunit/1&#039;&amp;gt;14 beta-sheets&amp;lt;/scene&amp;gt; (61 residues).&lt;br /&gt;
Chain B is formed of &amp;lt;scene name=&#039;82/829361/Helixchainb_asymunit/1&#039;&amp;gt;17 helices&amp;lt;/scene&amp;gt; (involving 218 residues) and &amp;lt;scene name=&#039;82/829361/Betasheetchainb_asymunit/1&#039;&amp;gt;14 beta-sheets&amp;lt;/scene&amp;gt; (62 residues). &lt;br /&gt;
&lt;br /&gt;
1% of the unit&#039;s amino acid have incomplete sidechains, which means that there are 11 missing residue in the assymetric unit.&amp;lt;ref&amp;gt;https://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4iv6&amp;lt;/ref&amp;gt;&lt;br /&gt;
&lt;br /&gt;
==Tertiary structures==&lt;br /&gt;
&lt;br /&gt;
The assymetric unit contains 2 ligands: 2FDA, Dihydroflavine-adenine dinucleotide.&lt;br /&gt;
The protein is a tetramer,the surface between the two monomers of a single dimer of an acyl-CoA dehydrogenase contains the FAD binding sites and has extensive bonding interactions. There are 2 active sites in the tetramer, each of these 2 sites contains a FAD molecule and an acyl-CoA substrate binding site. &amp;lt;ref&amp;gt;https://en.wikipedia.org/wiki/Flavin_adenine_dinucleotide&amp;lt;/ref&amp;gt;&lt;br /&gt;
&lt;br /&gt;
==Enzymatic reaction&amp;lt;ref&amp;gt;http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl?pdbcode=4iv6&amp;lt;/ref&amp;gt;&amp;lt;ref&amp;gt;https://www.ebi.ac.uk/intenz/query?cmd=SearchEC&amp;amp;ec=1.3.8.1&amp;lt;/ref&amp;gt;&amp;lt;ref&amp;gt;https://enzyme.expasy.org/EC/1.3.8.1&amp;lt;/ref&amp;gt;==&lt;br /&gt;
&lt;br /&gt;
[[Enzyme accepted name]]: Short-chain acyl-CoA dehydrogenase&lt;br /&gt;
&lt;br /&gt;
[[Other names]]:Butanoyl-CoA dehydrogenase, Butyryl dehydrogenase, Short-chain acyl CoA dehydrogenase, Unsatured acyl-CoA reductase.&lt;br /&gt;
&lt;br /&gt;
[[Enzyme class]]: E.C.1.3.8.1[https://enzyme.expasy.org/EC/1.3.8.1]&lt;br /&gt;
&lt;br /&gt;
[[Substrate]]: A short-chain acyl CoA &lt;br /&gt;
&lt;br /&gt;
[[Prosthetic group]]: 1 electron-transfer flavoprotein such as FDA, for every Subunits &lt;br /&gt;
&lt;br /&gt;
[[Products]]: a short-chain trans-2,3-dehydroacyl-CoA + reduced electron-transfer flavoprotein&lt;br /&gt;
&lt;br /&gt;
[[Informed Pathways]]: Fatty acid degradation&lt;br /&gt;
&lt;br /&gt;
[[Other information]]:&lt;br /&gt;
&lt;br /&gt;
The enzyme from beef liver can accept acyl-chain lengths from 3 to 8 carbon atoms. From different organism the range can vary so we ignore if &#039;&#039;Mycobacterium tuberculosis&#039;&#039; gets the same lengths resolution.&lt;br /&gt;
&lt;br /&gt;
The highest activity reported for beef liver enzyme was for substrates with 4 and 5 carbon acyl-chain lengths.&lt;br /&gt;
&lt;br /&gt;
==4IV6 as a research tool==&lt;br /&gt;
&lt;br /&gt;
4iv6 which belong to &#039;&#039;Mycobacterium tuberculosis&#039;&#039; was studied with other protein homolog.&lt;br /&gt;
They were chosen to be studied as potential TB-Drugs target&lt;br /&gt;
Studies have been made on homolog similarities aimed on their active site because with the knowledges of many homolog active site structure and how they work, we can design a inhibitor of those enzyme which can stop essential reaction and reduce or stop &#039;&#039;Mycobacterium tuberculosis&#039;&#039; infection.&lt;br /&gt;
This strategy is called an « Homolog-rescue strategy ».&lt;br /&gt;
This strategy can be generalized for other drug target for other diseases.&lt;br /&gt;
&lt;br /&gt;
&lt;br /&gt;
== Structural highlights summary ==&lt;br /&gt;
&lt;br /&gt;
&amp;lt;scene name=&#039;82/829361/Biological_unit/1&#039;&amp;gt;Biological unit&amp;lt;/scene&amp;gt;&lt;br /&gt;
&lt;br /&gt;
&amp;lt;scene name=&#039;82/829361/2asymunit/1&#039;&amp;gt;Asymmetric units&amp;lt;/scene&amp;gt;&lt;br /&gt;
&lt;br /&gt;
&amp;lt;scene name=&#039;82/829361/Betasheetchaina_asymunit/1&#039;&amp;gt;Beta-sheets&amp;lt;/scene&amp;gt;&lt;br /&gt;
&lt;br /&gt;
&amp;lt;scene name=&#039;82/829361/Helixalphachaina_asymunit/1&#039;&amp;gt;Helices&amp;lt;/scene&amp;gt;&lt;br /&gt;
&lt;br /&gt;
&amp;lt;scene name=&#039;82/829361/Secondary_structure/1&#039;&amp;gt;Secondary structure&amp;lt;/scene&amp;gt;  &lt;br /&gt;
&lt;br /&gt;
&amp;lt;scene name=&#039;82/829361/Chainea_asymunit/2&#039;&amp;gt;A chain&amp;lt;/scene&amp;gt; &lt;br /&gt;
&lt;br /&gt;
&amp;lt;scene name=&#039;82/829361/Chaineb_asymunit/1&#039;&amp;gt;B chain&amp;lt;/scene&amp;gt;&lt;br /&gt;
&lt;br /&gt;
&amp;lt;scene name=&#039;82/829361/Hydrophobic/1&#039;&amp;gt;Hydrophobic region&amp;lt;/scene&amp;gt;&lt;br /&gt;
&lt;br /&gt;
&amp;lt;/StructureSection&amp;gt;&lt;br /&gt;
== References ==&lt;br /&gt;
&amp;lt;references/&amp;gt;&lt;/div&gt;</summary>
		<author><name>Appoline Dubois</name></author>
	</entry>
	<entry>
		<id>https://proteopedia.org/index.php?title=Sandbox_Reserved_1108&amp;diff=3144187</id>
		<title>Sandbox Reserved 1108</title>
		<link rel="alternate" type="text/html" href="https://proteopedia.org/index.php?title=Sandbox_Reserved_1108&amp;diff=3144187"/>
		<updated>2020-01-17T15:41:24Z</updated>

		<summary type="html">&lt;p&gt;Appoline Dubois: &lt;/p&gt;
&lt;hr /&gt;
&lt;div&gt;{{Sandbox_ESBS_2019}}&amp;lt;!-- PLEASE ADD YOUR CONTENT BELOW HERE --&amp;gt;&lt;br /&gt;
==4iv6==&lt;br /&gt;
&amp;lt;StructureSection load=&#039;1stp&#039; size=&#039;340&#039; side=&#039;right&#039; caption=&#039;Caption for this structure&#039; scene=&#039;&#039;&amp;gt;&lt;br /&gt;
4iv6 is an  enzyme &#039;&#039;Mycobacterium tuberculosis&#039;&#039; which get his structure analyzed by Baugh et al. [https://www.ncbi.nlm.nih.gov/pubmed/25613812] with other enzymes homologue in order to fight &#039;&#039;Mycobacterium tuberculosis&#039;&#039; relative infections.&lt;br /&gt;
&lt;br /&gt;
== Function ==&lt;br /&gt;
4iv6 functions were not studied and only structural infos are disponible.&lt;br /&gt;
Nevertheless we can consider datas from other E.C.1.3.8.1[https://enzyme.expasy.org/EC/1.3.8.1] which came from other organisms.&lt;br /&gt;
E.C.1.3.8.1[https://enzyme.expasy.org/EC/1.3.8.1] is communly found in following pathways with various functions:&lt;br /&gt;
&lt;br /&gt;
[[Analine metabolism]]:[https://www.brenda-enzymes.info/pathway_index.php?pathway=alanine%20metabolism&amp;amp;ecno=1.3.8.1]&lt;br /&gt;
&lt;br /&gt;
[[Butanoate metabolism]]:[https://www.genome.jp/kegg-bin/show_pathway?map00650+1.3.8.1]&lt;br /&gt;
&lt;br /&gt;
[[Lipids metabolism]] : [https://www.brenda-enzymes.info/pathway_index.php?pathway=lipid%20metabolism&amp;amp;ecno=1.3.8.1][https://www.genome.jp/kegg-bin/show_pathway?map00071+1.3.8.1]&lt;br /&gt;
&lt;br /&gt;
[[Valine Leucine and isoleucine pathways]]:[https://www.genome.jp/kegg-bin/show_pathway?map00280+1.3.8.1]&lt;br /&gt;
&lt;br /&gt;
&lt;br /&gt;
==Primary and Secondary structure&amp;lt;ref&amp;gt;http://www.rcsb.org/structure/4IV6&amp;lt;/ref&amp;gt;==&lt;br /&gt;
&lt;br /&gt;
Isovaleryl-CoA dehydrogenase is the assembly of &#039;&#039;&#039;&amp;lt;scene name=&#039;82/829361/2asymunit/1&#039;&amp;gt;two asymmetric units&amp;lt;/scene&amp;gt;&#039;&#039;&#039; each composed of &#039;&#039;&#039;two chains &amp;lt;scene name=&#039;82/829361/Chainea_asymunit/2&#039;&amp;gt;A&amp;lt;/scene&amp;gt; and &amp;lt;scene name=&#039;82/829361/Chaineb_asymunit/1&#039;&amp;gt;B&amp;lt;/scene&amp;gt;&#039;&#039;&#039; linked by a &amp;lt;scene name=&#039;82/829361/Ligand_asymunit/1&#039;&amp;gt;ligand&amp;lt;/scene&amp;gt; (Dihydroflavine-Adenine Dinucleotide also known as [https://pubchem.ncbi.nlm.nih.gov/compound/Dihydroflavine-adenine-dinucleotide FADH2] ). Each of the two chains A and B are composed of 388 amino acids. An asymmetric unit is therefore composed of 776 amino acids and has a molecular weight of 86233.70 Da.&lt;br /&gt;
&lt;br /&gt;
The A chain is made up of &amp;lt;scene name=&#039;82/829361/Helixalphachaina_asymunit/1&#039;&amp;gt;17 helices&amp;lt;/scene&amp;gt; (involving 221 residues) and &amp;lt;scene name=&#039;82/829361/Betasheetchaina_asymunit/1&#039;&amp;gt;14 beta-sheets&amp;lt;/scene&amp;gt; (61 residues).&lt;br /&gt;
Chain B is formed of &amp;lt;scene name=&#039;82/829361/Helixchainb_asymunit/1&#039;&amp;gt;17 helices&amp;lt;/scene&amp;gt; (involving 218 residues) and &amp;lt;scene name=&#039;82/829361/Betasheetchainb_asymunit/1&#039;&amp;gt;14 beta-sheets&amp;lt;/scene&amp;gt; (62 residues). &lt;br /&gt;
&lt;br /&gt;
==Tertiary structures==&lt;br /&gt;
&lt;br /&gt;
Isovaleryl-CoA dehydrogenase from Mycobacterium smegmatis assymetric unit is composed of two chains. These two chains are sequence-identical. 765 amino acid alpha carbons are present in the model. 11 (1%) have incomplete sidechains, which means that there are 11 missing residue in the assymetric unit. The unit contains 6 580 atoms, with 5 different atoms: C, N, O, P, S. &amp;lt;ref&amp;gt;https://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4iv6&amp;lt;/ref&amp;gt;&lt;br /&gt;
The assymetric unit also contains 2 ligands: 2FDA, Dihydroflavine-adenine dinucleotide.&lt;br /&gt;
The protein is a tetramer,the surface between the two monomers of a single dimer of an acyl-CoA dehydrogenase contains the FAD binding sites and has extensive bonding interactions. There are 2 active sites in the tetramer, each of these 2 sites contains a FAD molecule and an acyl-CoA substrate binding site. &amp;lt;ref&amp;gt;https://en.wikipedia.org/wiki/Flavin_adenine_dinucleotide&amp;lt;/ref&amp;gt;&lt;br /&gt;
&lt;br /&gt;
==Enzymatic reaction&amp;lt;ref&amp;gt;http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl?pdbcode=4iv6&amp;lt;/ref&amp;gt;&amp;lt;ref&amp;gt;https://www.ebi.ac.uk/intenz/query?cmd=SearchEC&amp;amp;ec=1.3.8.1&amp;lt;/ref&amp;gt;&amp;lt;ref&amp;gt;https://enzyme.expasy.org/EC/1.3.8.1&amp;lt;/ref&amp;gt;==&lt;br /&gt;
&lt;br /&gt;
[[Enzyme accepted name]]: Short-chain acyl-CoA dehydrogenase&lt;br /&gt;
&lt;br /&gt;
[[Other names]]:Butanoyl-CoA dehydrogenase, Butyryl dehydrogenase, Short-chain acyl CoA dehydrogenase, Unsatured acyl-CoA reductase.&lt;br /&gt;
&lt;br /&gt;
[[Enzyme class]]: E.C.1.3.8.1[https://enzyme.expasy.org/EC/1.3.8.1]&lt;br /&gt;
&lt;br /&gt;
[[Substrate]]: A short-chain acyl CoA &lt;br /&gt;
&lt;br /&gt;
[[Prosthetic group]]: 1 electron-transfer flavoprotein such as FDA, for every Subunits &lt;br /&gt;
&lt;br /&gt;
[[Products]]: a short-chain trans-2,3-dehydroacyl-CoA + reduced electron-transfer flavoprotein&lt;br /&gt;
&lt;br /&gt;
[[Informed Pathways]]: Fatty acid degradation&lt;br /&gt;
&lt;br /&gt;
[[Other information]]:&lt;br /&gt;
&lt;br /&gt;
The enzyme from beef liver can accept acyl-chain lengths from 3 to 8 carbon atoms. From different organism the range can vary so we ignore if &#039;&#039;Mycobacterium tuberculosis&#039;&#039; gets the same lengths resolution.&lt;br /&gt;
&lt;br /&gt;
The highest activity reported for beef liver enzyme was for substrates with 4 and 5 carbon acyl-chain lengths.&lt;br /&gt;
&lt;br /&gt;
==4IV6 as a research tool==&lt;br /&gt;
&lt;br /&gt;
4iv6 which belong to &#039;&#039;Mycobacterium tuberculosis&#039;&#039; was studied with other protein homolog.&lt;br /&gt;
They were chosen to be studied as potential TB-Drugs target&lt;br /&gt;
Studies have been made on homolog similarities aimed on their active site because with the knowledges of many homolog active site structure and how they work, we can design a inhibitor of those enzyme which can stop essential reaction and reduce or stop &#039;&#039;Mycobacterium tuberculosis&#039;&#039; infection.&lt;br /&gt;
This strategy is called an « Homolog-rescue strategy ».&lt;br /&gt;
This strategy can be generalized for other drug target for other diseases.&lt;br /&gt;
&lt;br /&gt;
&lt;br /&gt;
== Structural highlights summary ==&lt;br /&gt;
&lt;br /&gt;
&amp;lt;scene name=&#039;82/829361/Biological_unit/1&#039;&amp;gt;Biological unit&amp;lt;/scene&amp;gt;&lt;br /&gt;
&lt;br /&gt;
&amp;lt;scene name=&#039;82/829361/2asymunit/1&#039;&amp;gt;Asymmetric units&amp;lt;/scene&amp;gt;&lt;br /&gt;
&lt;br /&gt;
&amp;lt;scene name=&#039;82/829361/Betasheetchaina_asymunit/1&#039;&amp;gt;Beta-sheets&amp;lt;/scene&amp;gt;&lt;br /&gt;
&lt;br /&gt;
&amp;lt;scene name=&#039;82/829361/Helixalphachaina_asymunit/1&#039;&amp;gt;Helices&amp;lt;/scene&amp;gt;&lt;br /&gt;
&lt;br /&gt;
&amp;lt;scene name=&#039;82/829361/Secondary_structure/1&#039;&amp;gt;Secondary structure&amp;lt;/scene&amp;gt;  &lt;br /&gt;
&lt;br /&gt;
&amp;lt;scene name=&#039;82/829361/Chainea_asymunit/2&#039;&amp;gt;A chain&amp;lt;/scene&amp;gt; &lt;br /&gt;
&lt;br /&gt;
&amp;lt;scene name=&#039;82/829361/Chaineb_asymunit/1&#039;&amp;gt;B chain&amp;lt;/scene&amp;gt;&lt;br /&gt;
&lt;br /&gt;
&amp;lt;scene name=&#039;82/829361/Hydrophobic/1&#039;&amp;gt;Hydrophobic region&amp;lt;/scene&amp;gt;&lt;br /&gt;
&lt;br /&gt;
&amp;lt;/StructureSection&amp;gt;&lt;br /&gt;
== References ==&lt;br /&gt;
&amp;lt;references/&amp;gt;&lt;/div&gt;</summary>
		<author><name>Appoline Dubois</name></author>
	</entry>
	<entry>
		<id>https://proteopedia.org/index.php?title=Sandbox_Reserved_1108&amp;diff=3144185</id>
		<title>Sandbox Reserved 1108</title>
		<link rel="alternate" type="text/html" href="https://proteopedia.org/index.php?title=Sandbox_Reserved_1108&amp;diff=3144185"/>
		<updated>2020-01-17T15:38:09Z</updated>

		<summary type="html">&lt;p&gt;Appoline Dubois: &lt;/p&gt;
&lt;hr /&gt;
&lt;div&gt;{{Sandbox_ESBS_2019}}&amp;lt;!-- PLEASE ADD YOUR CONTENT BELOW HERE --&amp;gt;&lt;br /&gt;
==4iv6==&lt;br /&gt;
&amp;lt;StructureSection load=&#039;1stp&#039; size=&#039;340&#039; side=&#039;right&#039; caption=&#039;Caption for this structure&#039; scene=&#039;&#039;&amp;gt;&lt;br /&gt;
4iv6 is an  enzyme &#039;&#039;Mycobacterium tuberculosis&#039;&#039; which get his structure analyzed by Baugh et al. [https://www.ncbi.nlm.nih.gov/pubmed/25613812] with other enzymes homologue in order to fight &#039;&#039;Mycobacterium tuberculosis&#039;&#039; relative infections.&lt;br /&gt;
&lt;br /&gt;
== Function ==&lt;br /&gt;
4iv6 functions were not studied and only structural infos are disponible.&lt;br /&gt;
Nevertheless we can consider datas from other E.C.1.3.8.1[https://enzyme.expasy.org/EC/1.3.8.1] which came from other organisms.&lt;br /&gt;
E.C.1.3.8.1[https://enzyme.expasy.org/EC/1.3.8.1] is communly found in following pathways with various functions:&lt;br /&gt;
&lt;br /&gt;
[[Analine metabolism]]:[https://www.brenda-enzymes.info/pathway_index.php?pathway=alanine%20metabolism&amp;amp;ecno=1.3.8.1]&lt;br /&gt;
&lt;br /&gt;
[[Butanoate metabolism]]:[https://www.genome.jp/kegg-bin/show_pathway?map00650+1.3.8.1]&lt;br /&gt;
&lt;br /&gt;
[[Lipids metabolism]] : [https://www.brenda-enzymes.info/pathway_index.php?pathway=lipid%20metabolism&amp;amp;ecno=1.3.8.1][https://www.genome.jp/kegg-bin/show_pathway?map00071+1.3.8.1]&lt;br /&gt;
&lt;br /&gt;
[[Valine Leucine and isoleucine pathways]]:[https://www.genome.jp/kegg-bin/show_pathway?map00280+1.3.8.1]&lt;br /&gt;
&lt;br /&gt;
&lt;br /&gt;
==Primary and Secondary structure&amp;lt;ref&amp;gt;http://www.rcsb.org/structure/4IV6&amp;lt;/ref&amp;gt;==&lt;br /&gt;
&lt;br /&gt;
Isovaleryl-CoA dehydrogenase is the assembly of &#039;&#039;&#039;&amp;lt;scene name=&#039;82/829361/2asymunit/1&#039;&amp;gt;two asymmetric units&amp;lt;/scene&amp;gt;&#039;&#039;&#039; each composed of &#039;&#039;&#039;two chains &amp;lt;scene name=&#039;82/829361/Chainea_asymunit/2&#039;&amp;gt;A&amp;lt;/scene&amp;gt; and &amp;lt;scene name=&#039;82/829361/Chaineb_asymunit/1&#039;&amp;gt;B&amp;lt;/scene&amp;gt;&#039;&#039;&#039; linked by a &amp;lt;scene name=&#039;82/829361/Ligand_asymunit/1&#039;&amp;gt;ligand&amp;lt;/scene&amp;gt; (Dihydroflavine-Adenine Dinucleotide also known as [https://pubchem.ncbi.nlm.nih.gov/compound/Dihydroflavine-adenine-dinucleotide FADH2] ). Each of the two chains A and B are composed of 388 amino acids. An asymmetric unit is therefore composed of 776 amino acids and has a molecular weight of 86233.70 Da.&lt;br /&gt;
&lt;br /&gt;
The A chain is made up of &amp;lt;scene name=&#039;82/829361/Helixalphachaina_asymunit/1&#039;&amp;gt;17 helices&amp;lt;/scene&amp;gt; (involving 221 residues) and &amp;lt;scene name=&#039;82/829361/Betasheetchaina_asymunit/1&#039;&amp;gt;14 beta-sheets&amp;lt;/scene&amp;gt; (61 residues).&lt;br /&gt;
Chain B is formed of &amp;lt;scene name=&#039;82/829361/Helixchainb_asymunit/1&#039;&amp;gt;17 helices&amp;lt;/scene&amp;gt; (involving 218 residues) and &amp;lt;scene name=&#039;82/829361/Betasheetchainb_asymunit/1&#039;&amp;gt;14 beta-sheets&amp;lt;/scene&amp;gt; (62 residues). &lt;br /&gt;
&lt;br /&gt;
==Tertiary structures==&lt;br /&gt;
&lt;br /&gt;
Isovaleryl-CoA dehydrogenase from Mycobacterium smegmatis assymetric unit is composed of two chains. These two chains are sequence-identical. 765 amino acid alpha carbons are present in the model. 11 (1%) have incomplete sidechains, which means that there are 11 missing residue in the assymetric unit. The unit contains 6 580 atoms, with 5 different atoms: C, N, O, P, S. &lt;br /&gt;
The assymetric unit also contains 2 ligands: 2FDA, Dihydroflavine-adenine dinucleotide.&lt;br /&gt;
The protein is a tetramer,the surface between the two monomers of a single dimer of an acyl-CoA dehydrogenase contains the FAD binding sites and has extensive bonding interactions. There are 2 active sites in the tetramer, each of these 2 sites contains a FAD molecule and an acyl-CoA substrate binding site.&lt;br /&gt;
&lt;br /&gt;
==Enzymatic reaction&amp;lt;ref&amp;gt;http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl?pdbcode=4iv6&amp;lt;/ref&amp;gt;&amp;lt;ref&amp;gt;https://www.ebi.ac.uk/intenz/query?cmd=SearchEC&amp;amp;ec=1.3.8.1&amp;lt;/ref&amp;gt;&amp;lt;ref&amp;gt;https://enzyme.expasy.org/EC/1.3.8.1&amp;lt;/ref&amp;gt;==&lt;br /&gt;
&lt;br /&gt;
[[Enzyme accepted name]]: Short-chain acyl-CoA dehydrogenase&lt;br /&gt;
&lt;br /&gt;
[[Other names]]:Butanoyl-CoA dehydrogenase, Butyryl dehydrogenase, Short-chain acyl CoA dehydrogenase, Unsatured acyl-CoA reductase.&lt;br /&gt;
&lt;br /&gt;
[[Enzyme class]]: E.C.1.3.8.1[https://enzyme.expasy.org/EC/1.3.8.1]&lt;br /&gt;
&lt;br /&gt;
[[Substrate]]: A short-chain acyl CoA &lt;br /&gt;
&lt;br /&gt;
[[Prosthetic group]]: 1 electron-transfer flavoprotein such as FDA, for every Subunits &lt;br /&gt;
&lt;br /&gt;
[[Products]]: a short-chain trans-2,3-dehydroacyl-CoA + reduced electron-transfer flavoprotein&lt;br /&gt;
&lt;br /&gt;
[[Informed Pathways]]: Fatty acid degradation&lt;br /&gt;
&lt;br /&gt;
[[Other information]]:&lt;br /&gt;
&lt;br /&gt;
The enzyme from beef liver can accept acyl-chain lengths from 3 to 8 carbon atoms. From different organism the range can vary so we ignore if &#039;&#039;Mycobacterium tuberculosis&#039;&#039; gets the same lengths resolution.&lt;br /&gt;
&lt;br /&gt;
The highest activity reported for beef liver enzyme was for substrates with 4 and 5 carbon acyl-chain lengths.&lt;br /&gt;
&lt;br /&gt;
==4IV6 as a research tool==&lt;br /&gt;
&lt;br /&gt;
4iv6 which belong to &#039;&#039;Mycobacterium tuberculosis&#039;&#039; was studied with other protein homolog.&lt;br /&gt;
They were chosen to be studied as potential TB-Drugs target&lt;br /&gt;
Studies have been made on homolog similarities aimed on their active site because with the knowledges of many homolog active site structure and how they work, we can design a inhibitor of those enzyme which can stop essential reaction and reduce or stop &#039;&#039;Mycobacterium tuberculosis&#039;&#039; infection.&lt;br /&gt;
This strategy is called an « Homolog-rescue strategy ».&lt;br /&gt;
This strategy can be generalized for other drug target for other diseases.&lt;br /&gt;
&lt;br /&gt;
&lt;br /&gt;
== Structural highlights summary ==&lt;br /&gt;
&lt;br /&gt;
&amp;lt;scene name=&#039;82/829361/Biological_unit/1&#039;&amp;gt;Biological unit&amp;lt;/scene&amp;gt;&lt;br /&gt;
&lt;br /&gt;
&amp;lt;scene name=&#039;82/829361/2asymunit/1&#039;&amp;gt;Asymmetric units&amp;lt;/scene&amp;gt;&lt;br /&gt;
&lt;br /&gt;
&amp;lt;scene name=&#039;82/829361/Betasheetchaina_asymunit/1&#039;&amp;gt;Beta-sheets&amp;lt;/scene&amp;gt;&lt;br /&gt;
&lt;br /&gt;
&amp;lt;scene name=&#039;82/829361/Helixalphachaina_asymunit/1&#039;&amp;gt;Helices&amp;lt;/scene&amp;gt;&lt;br /&gt;
&lt;br /&gt;
&amp;lt;scene name=&#039;82/829361/Secondary_structure/1&#039;&amp;gt;Secondary structure&amp;lt;/scene&amp;gt;  &lt;br /&gt;
&lt;br /&gt;
&amp;lt;scene name=&#039;82/829361/Chainea_asymunit/2&#039;&amp;gt;A chain&amp;lt;/scene&amp;gt; &lt;br /&gt;
&lt;br /&gt;
&amp;lt;scene name=&#039;82/829361/Chaineb_asymunit/1&#039;&amp;gt;B chain&amp;lt;/scene&amp;gt;&lt;br /&gt;
&lt;br /&gt;
&amp;lt;scene name=&#039;82/829361/Hydrophobic/1&#039;&amp;gt;Hydrophobic region&amp;lt;/scene&amp;gt;&lt;br /&gt;
&lt;br /&gt;
&amp;lt;/StructureSection&amp;gt;&lt;br /&gt;
== References ==&lt;br /&gt;
&amp;lt;references/&amp;gt;&lt;/div&gt;</summary>
		<author><name>Appoline Dubois</name></author>
	</entry>
	<entry>
		<id>https://proteopedia.org/index.php?title=Sandbox_Reserved_1108&amp;diff=3144172</id>
		<title>Sandbox Reserved 1108</title>
		<link rel="alternate" type="text/html" href="https://proteopedia.org/index.php?title=Sandbox_Reserved_1108&amp;diff=3144172"/>
		<updated>2020-01-17T15:23:17Z</updated>

		<summary type="html">&lt;p&gt;Appoline Dubois: &lt;/p&gt;
&lt;hr /&gt;
&lt;div&gt;{{Sandbox_ESBS_2019}}&amp;lt;!-- PLEASE ADD YOUR CONTENT BELOW HERE --&amp;gt;&lt;br /&gt;
==4iv6==&lt;br /&gt;
&amp;lt;StructureSection load=&#039;1stp&#039; size=&#039;340&#039; side=&#039;right&#039; caption=&#039;Caption for this structure&#039; scene=&#039;&#039;&amp;gt;&lt;br /&gt;
4iv6 is an  enzyme &#039;&#039;Mycobacterium tuberculosis&#039;&#039; which get his structure analyzed by Baugh et al. [https://www.ncbi.nlm.nih.gov/pubmed/25613812] with other enzymes homologue in order to fight &#039;&#039;Mycobacterium tuberculosis&#039;&#039; relative infections.&lt;br /&gt;
&lt;br /&gt;
== Function ==&lt;br /&gt;
4iv6 functions were not studied and only structural infos are disponible.&lt;br /&gt;
Nevertheless we can consider datas from other E.C.1.3.8.1[https://enzyme.expasy.org/EC/1.3.8.1] which came from other organisms.&lt;br /&gt;
E.C.1.3.8.1[https://enzyme.expasy.org/EC/1.3.8.1] is communly found in following pathways with various functions:&lt;br /&gt;
&lt;br /&gt;
[[Analine metabolism]]:[https://www.brenda-enzymes.info/pathway_index.php?pathway=alanine%20metabolism&amp;amp;ecno=1.3.8.1]&lt;br /&gt;
&lt;br /&gt;
[[Butanoate metabolism]]:[https://www.genome.jp/kegg-bin/show_pathway?map00650+1.3.8.1]&lt;br /&gt;
&lt;br /&gt;
[[Lipids metabolism]] : [https://www.brenda-enzymes.info/pathway_index.php?pathway=lipid%20metabolism&amp;amp;ecno=1.3.8.1][https://www.genome.jp/kegg-bin/show_pathway?map00071+1.3.8.1]&lt;br /&gt;
&lt;br /&gt;
[[Valine Leucine and isoleucine pathways]]:[https://www.genome.jp/kegg-bin/show_pathway?map00280+1.3.8.1]&lt;br /&gt;
&lt;br /&gt;
&lt;br /&gt;
==Primary and Secondary structure&amp;lt;ref&amp;gt;http://www.rcsb.org/structure/4IV6&amp;lt;/ref&amp;gt;==&lt;br /&gt;
&lt;br /&gt;
Isovaleryl-CoA dehydrogenase is the assembly of &#039;&#039;&#039;&amp;lt;scene name=&#039;82/829361/2asymunit/1&#039;&amp;gt;two asymmetric units&amp;lt;/scene&amp;gt;&#039;&#039;&#039; each composed of &#039;&#039;&#039;two chains &amp;lt;scene name=&#039;82/829361/Chainea_asymunit/2&#039;&amp;gt;A&amp;lt;/scene&amp;gt; and &amp;lt;scene name=&#039;82/829361/Chaineb_asymunit/1&#039;&amp;gt;B&amp;lt;/scene&amp;gt;&#039;&#039;&#039; linked by a &amp;lt;scene name=&#039;82/829361/Ligand_asymunit/1&#039;&amp;gt;ligand&amp;lt;/scene&amp;gt; (Dihydroflavine-Adenine Dinucleotide also known as [https://pubchem.ncbi.nlm.nih.gov/compound/Dihydroflavine-adenine-dinucleotide FADH2] ). Each of the two chains A and B are composed of 388 amino acids. An asymmetric unit is therefore composed of 776 amino acids and has a molecular weight of 86233.70 Da.&lt;br /&gt;
&lt;br /&gt;
The A chain is made up of &amp;lt;scene name=&#039;82/829361/Helixalphachaina_asymunit/1&#039;&amp;gt;17 helices&amp;lt;/scene&amp;gt; (involving 221 residues) and &amp;lt;scene name=&#039;82/829361/Betasheetchaina_asymunit/1&#039;&amp;gt;14 beta-sheets&amp;lt;/scene&amp;gt; (61 residues).&lt;br /&gt;
Chain B is formed of &amp;lt;scene name=&#039;82/829361/Helixchainb_asymunit/1&#039;&amp;gt;17 helices&amp;lt;/scene&amp;gt; (involving 218 residues) and &amp;lt;scene name=&#039;82/829361/Betasheetchainb_asymunit/1&#039;&amp;gt;14 beta-sheets&amp;lt;/scene&amp;gt; (62 residues). &lt;br /&gt;
&lt;br /&gt;
==Tertiary structures==&lt;br /&gt;
&lt;br /&gt;
Isovaleryl-CoA dehydrogenase from Mycobacterium smegmatis assymetric unit is composed of two chains. These two chains are sequence-identical. 765 amino acid alpha carbons are present in the model. 11 (1%) have incomplete sidechains, which means that there are 11 missing residue in the assymetric unit. The unit contains 6 580 atoms, with 5 different atoms: C, N, O, P, S. &lt;br /&gt;
The assymetric unit also contains 2 ligands: 2FDA, Dihydroflavine-adenine dinucleotide.&lt;br /&gt;
&lt;br /&gt;
==Enzymatic reaction&amp;lt;ref&amp;gt;http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl?pdbcode=4iv6&amp;lt;/ref&amp;gt;&amp;lt;ref&amp;gt;https://www.ebi.ac.uk/intenz/query?cmd=SearchEC&amp;amp;ec=1.3.8.1&amp;lt;/ref&amp;gt;&amp;lt;ref&amp;gt;https://enzyme.expasy.org/EC/1.3.8.1&amp;lt;/ref&amp;gt;==&lt;br /&gt;
&lt;br /&gt;
[[Enzyme accepted name]]: Short-chain acyl-CoA dehydrogenase&lt;br /&gt;
&lt;br /&gt;
[[Other names]]:Butanoyl-CoA dehydrogenase, Butyryl dehydrogenase, Short-chain acyl CoA dehydrogenase, Unsatured acyl-CoA reductase.&lt;br /&gt;
&lt;br /&gt;
[[Enzyme class]]: E.C.1.3.8.1[https://enzyme.expasy.org/EC/1.3.8.1]&lt;br /&gt;
&lt;br /&gt;
[[Substrate]]: A short-chain acyl CoA &lt;br /&gt;
&lt;br /&gt;
[[Prosthetic group]]: 1 electron-transfer flavoprotein such as FDA, for every Subunits &lt;br /&gt;
&lt;br /&gt;
[[Products]]: a short-chain trans-2,3-dehydroacyl-CoA + reduced electron-transfer flavoprotein&lt;br /&gt;
&lt;br /&gt;
[[Informed Pathways]]: Fatty acid degradation&lt;br /&gt;
&lt;br /&gt;
[[Other information]]:&lt;br /&gt;
&lt;br /&gt;
The enzyme from beef liver can accept acyl-chain lengths from 3 to 8 carbon atoms. From different organism the range can vary so we ignore if &#039;&#039;Mycobacterium tuberculosis&#039;&#039; gets the same lengths resolution.&lt;br /&gt;
&lt;br /&gt;
The highest activity reported for beef liver enzyme was for substrates with 4 and 5 carbon acyl-chain lengths.&lt;br /&gt;
&lt;br /&gt;
==4IV6 as a research tool==&lt;br /&gt;
&lt;br /&gt;
4iv6 which belong to &#039;&#039;Mycobacterium tuberculosis&#039;&#039; was studied with other protein homolog.&lt;br /&gt;
They were chosen to be studied as potential TB-Drugs target&lt;br /&gt;
Studies have been made on homolog similarities aimed on their active site because with the knowledges of many homolog active site structure and how they work, we can design a inhibitor of those enzyme which can stop essential reaction and reduce or stop &#039;&#039;Mycobacterium tuberculosis&#039;&#039; infection.&lt;br /&gt;
This strategy is called an « Homolog-rescue strategy ».&lt;br /&gt;
This strategy can be generalized for other drug target for other diseases.&lt;br /&gt;
&lt;br /&gt;
&lt;br /&gt;
== Structural highlights summary ==&lt;br /&gt;
&lt;br /&gt;
&amp;lt;scene name=&#039;82/829361/Biological_unit/1&#039;&amp;gt;Biological unit&amp;lt;/scene&amp;gt;&lt;br /&gt;
&lt;br /&gt;
&amp;lt;scene name=&#039;82/829361/2asymunit/1&#039;&amp;gt;Asymmetric units&amp;lt;/scene&amp;gt;&lt;br /&gt;
&lt;br /&gt;
&amp;lt;scene name=&#039;82/829361/Betasheetchaina_asymunit/1&#039;&amp;gt;Beta-sheets&amp;lt;/scene&amp;gt;&lt;br /&gt;
&lt;br /&gt;
&amp;lt;scene name=&#039;82/829361/Helixalphachaina_asymunit/1&#039;&amp;gt;Helices&amp;lt;/scene&amp;gt;&lt;br /&gt;
&lt;br /&gt;
&amp;lt;scene name=&#039;82/829361/Secondary_structure/1&#039;&amp;gt;Secondary structure&amp;lt;/scene&amp;gt;  &lt;br /&gt;
&lt;br /&gt;
&amp;lt;scene name=&#039;82/829361/Chainea_asymunit/2&#039;&amp;gt;A chain&amp;lt;/scene&amp;gt; &lt;br /&gt;
&lt;br /&gt;
&amp;lt;scene name=&#039;82/829361/Chaineb_asymunit/1&#039;&amp;gt;B chain&amp;lt;/scene&amp;gt;&lt;br /&gt;
&lt;br /&gt;
&amp;lt;scene name=&#039;82/829361/Hydrophobic/1&#039;&amp;gt;Hydrophobic region&amp;lt;/scene&amp;gt;&lt;br /&gt;
&lt;br /&gt;
&amp;lt;/StructureSection&amp;gt;&lt;br /&gt;
== References ==&lt;br /&gt;
&amp;lt;references/&amp;gt;&lt;/div&gt;</summary>
		<author><name>Appoline Dubois</name></author>
	</entry>
	<entry>
		<id>https://proteopedia.org/index.php?title=Sandbox_Reserved_1108&amp;diff=3143151</id>
		<title>Sandbox Reserved 1108</title>
		<link rel="alternate" type="text/html" href="https://proteopedia.org/index.php?title=Sandbox_Reserved_1108&amp;diff=3143151"/>
		<updated>2020-01-14T18:06:03Z</updated>

		<summary type="html">&lt;p&gt;Appoline Dubois: &lt;/p&gt;
&lt;hr /&gt;
&lt;div&gt;{{Sandbox_ESBS_2019}}&amp;lt;!-- PLEASE ADD YOUR CONTENT BELOW HERE --&amp;gt;&lt;br /&gt;
==Your Heading Here (maybe something like &#039;Structure&#039;)==&lt;br /&gt;
&amp;lt;StructureSection load=&#039;1stp&#039; size=&#039;340&#039; side=&#039;right&#039; caption=&#039;Caption for this structure&#039; scene=&#039;&#039;&amp;gt;&lt;br /&gt;
This is a default text for your page &#039;&#039;&#039;&#039;&#039;&#039;. Click above on &#039;&#039;&#039;edit this page&#039;&#039;&#039; to modify. Be careful with the &amp;amp;lt; and &amp;amp;gt; signs.&lt;br /&gt;
You may include any references to papers as in: the use of JSmol in Proteopedia &amp;lt;ref&amp;gt;DOI 10.1002/ijch.201300024&amp;lt;/ref&amp;gt; or to the article describing Jmol &amp;lt;ref&amp;gt;PMID:21638687&amp;lt;/ref&amp;gt; to the rescue.&lt;br /&gt;
&lt;br /&gt;
== Function ==&lt;br /&gt;
==Primary and Secondary structure&amp;lt;ref&amp;gt;http://www.rcsb.org/structure/4IV6&amp;lt;/ref&amp;gt;==&lt;br /&gt;
&lt;br /&gt;
Isovaleryl-CoA dehydrogenase is the assembly of &#039;&#039;&#039;&amp;lt;scene name=&#039;82/829361/2asymunit/1&#039;&amp;gt;two asymmetric units&amp;lt;/scene&amp;gt;&#039;&#039;&#039; each composed of &#039;&#039;&#039;two chains &amp;lt;scene name=&#039;82/829361/Chainea_asymunit/2&#039;&amp;gt;A&amp;lt;/scene&amp;gt; and &amp;lt;scene name=&#039;82/829361/Chaineb_asymunit/1&#039;&amp;gt;B&amp;lt;/scene&amp;gt;&#039;&#039;&#039; linked by a &amp;lt;scene name=&#039;82/829361/Ligand_asymunit/1&#039;&amp;gt;ligand&amp;lt;/scene&amp;gt; (Dihydroflavine-Adenine Dinucleotide also known as  	 [https://pubchem.ncbi.nlm.nih.gov/compound/Dihydroflavine-adenine-dinucleotide FADH2] ). Each of the two chains A and B are composed of 388 amino acids. An asymmetric unit is therefore composed of 776 amino acids and has a molecular weight of 86233.70 Da.&lt;br /&gt;
&lt;br /&gt;
The A chain is made up of &amp;lt;scene name=&#039;82/829361/Helixalphachaina_asymunit/1&#039;&amp;gt;17 helices&amp;lt;/scene&amp;gt; (involving 221 residues) and &amp;lt;scene name=&#039;82/829361/Betasheetchaina_asymunit/1&#039;&amp;gt;14 beta-sheets&amp;lt;/scene&amp;gt; (61 residues).&lt;br /&gt;
Chain B is formed of &amp;lt;scene name=&#039;82/829361/Helixchainb_asymunit/1&#039;&amp;gt;17 helices&amp;lt;/scene&amp;gt; (involving 218 residues) and &amp;lt;scene name=&#039;82/829361/Betasheetchainb_asymunit/1&#039;&amp;gt;14 beta-sheets&amp;lt;/scene&amp;gt; (62 residues). &lt;br /&gt;
&lt;br /&gt;
==Tertiary structures==&lt;br /&gt;
==Enzymatic reaction==&lt;br /&gt;
&lt;br /&gt;
[[Enzyme accepted name]]: Short-chain acyl-CoA dehydrogenase&lt;br /&gt;
&lt;br /&gt;
[[Other names]]:Butanoyl-CoA dehydrogenase, Butyryl dehydrogenase, Short-chain acyl CoA dehydrogenase, Unsatured acyl-CoA reductase.&lt;br /&gt;
&lt;br /&gt;
[[Enzyme class]]: E.C.1.3.8.1[https://enzyme.expasy.org/EC/1.3.8.1]&lt;br /&gt;
&lt;br /&gt;
[[Substrate]]: A short-chain acyl CoA &lt;br /&gt;
&lt;br /&gt;
[[Prosthetic group]]: 1 electron-transfer flavoprotein such as FDA, for every Subunits &lt;br /&gt;
&lt;br /&gt;
[[Products]]: a short-chain trans-2,3-dehydroacyl-CoA + reduced electron-transfer flavoprotein&lt;br /&gt;
&lt;br /&gt;
[[Pathways]]: Fatty acid degradation&lt;br /&gt;
&lt;br /&gt;
[[Other information]]:&lt;br /&gt;
&lt;br /&gt;
The enzyme from beef liver can accept acyl-chain lengths from 3 to 8 carbon atoms. From different organism the range can vary so we ignore if M.tuberculosis gets the same lengths resolution.&lt;br /&gt;
&lt;br /&gt;
The highest activity reported for beef liver enzyme was for substrates with 4 and 5 carbon acyl-chain lengths.&lt;br /&gt;
&lt;br /&gt;
==4IV6 as a research tool==&lt;br /&gt;
&lt;br /&gt;
4iv6 which belong to &#039;&#039;Mycobacterium tuberculosis&#039;&#039; was studied with other protein homolog.&lt;br /&gt;
They were chosen to be studied as potential TB-Drugs target&lt;br /&gt;
Studies have been made on homolog similarities aimed on their active site because with the knowledges of many homolog active site structure and how they work, we can design a inhibitor of those enzyme which can stop essential reaction and reduce or stop &#039;&#039;M.tuberculosis&#039;&#039; infection.&lt;br /&gt;
This strategy is called an « Homolog-rescue strategy ».&lt;br /&gt;
This strategy can be generalized for other drug target for other diseases.&lt;br /&gt;
&lt;br /&gt;
&lt;br /&gt;
== Structural highlights ==&lt;br /&gt;
&amp;lt;scene name=&#039;82/829361/Biological_unit/1&#039;&amp;gt;Biological unit&amp;lt;/scene&amp;gt;&lt;br /&gt;
&lt;br /&gt;
&amp;lt;scene name=&#039;82/829361/Asymetrical_unit/2&#039;&amp;gt;Asymetrical unit&amp;lt;/scene&amp;gt; :Light Grey:1st sub-unit, Light green:2nd sub-unit, Blue and red:FDA &lt;br /&gt;
&lt;br /&gt;
&amp;lt;scene name=&#039;82/829361/Secondary_structure/1&#039;&amp;gt;Secondary structure&amp;lt;/scene&amp;gt; : Red: helix alpha, Blue:FDA, Yellow: Beta sheet  &lt;br /&gt;
&lt;br /&gt;
&amp;lt;scene name=&#039;82/829361/Hydrophobic/1&#039;&amp;gt;Hydrophobic region&amp;lt;/scene&amp;gt; : Green: FDA, Purple: Polar region, Light grey: Hydrophobic region &lt;br /&gt;
&lt;br /&gt;
&amp;lt;/StructureSection&amp;gt;&lt;br /&gt;
== References ==&lt;br /&gt;
&amp;lt;references/&amp;gt;&lt;/div&gt;</summary>
		<author><name>Appoline Dubois</name></author>
	</entry>
	<entry>
		<id>https://proteopedia.org/index.php?title=Sandbox_Reserved_1108&amp;diff=3143148</id>
		<title>Sandbox Reserved 1108</title>
		<link rel="alternate" type="text/html" href="https://proteopedia.org/index.php?title=Sandbox_Reserved_1108&amp;diff=3143148"/>
		<updated>2020-01-14T18:05:27Z</updated>

		<summary type="html">&lt;p&gt;Appoline Dubois: &lt;/p&gt;
&lt;hr /&gt;
&lt;div&gt;{{Sandbox_ESBS_2019}}&amp;lt;!-- PLEASE ADD YOUR CONTENT BELOW HERE --&amp;gt;&lt;br /&gt;
==Your Heading Here (maybe something like &#039;Structure&#039;)==&lt;br /&gt;
&#039;&#039;&amp;lt;StructureSection load=&#039;1stp&#039; size=&#039;340&#039; side=&#039;right&#039; caption=&#039;Caption for this structure&#039; scene=&#039;&#039;&amp;gt;&lt;br /&gt;
This is a default text for your page &#039;&#039;&#039;&#039;&#039;&#039;. Click above on &#039;&#039;&#039;edit this page&#039;&#039;&#039; to modify. Be careful with the &amp;amp;lt; and &amp;amp;gt; signs.&lt;br /&gt;
You may include any references to papers as in: the use of JSmol in Proteopedia &amp;lt;ref&amp;gt;DOI 10.1002/ijch.201300024&amp;lt;/ref&amp;gt; or to the article describing Jmol &amp;lt;ref&amp;gt;PMID:21638687&amp;lt;/ref&amp;gt; to the rescue.&#039;&#039;&lt;br /&gt;
&lt;br /&gt;
== Function ==&lt;br /&gt;
==Primary and Secondary structure&amp;lt;ref&amp;gt;http://www.rcsb.org/structure/4IV6&amp;lt;/ref&amp;gt;==&lt;br /&gt;
&lt;br /&gt;
Isovaleryl-CoA dehydrogenase is the assembly of &#039;&#039;&#039;&amp;lt;scene name=&#039;82/829361/2asymunit/1&#039;&amp;gt;two asymmetric units&amp;lt;/scene&amp;gt;&#039;&#039;&#039; each composed of &#039;&#039;&#039;two chains &amp;lt;scene name=&#039;82/829361/Chainea_asymunit/2&#039;&amp;gt;A&amp;lt;/scene&amp;gt; and &amp;lt;scene name=&#039;82/829361/Chaineb_asymunit/1&#039;&amp;gt;B&amp;lt;/scene&amp;gt;&#039;&#039;&#039; linked by a &amp;lt;scene name=&#039;82/829361/Ligand_asymunit/1&#039;&amp;gt;ligand&amp;lt;/scene&amp;gt; (Dihydroflavine-Adenine Dinucleotide also known as  	 [https://pubchem.ncbi.nlm.nih.gov/compound/Dihydroflavine-adenine-dinucleotide FADH2] ). Each of the two chains A and B are composed of 388 amino acids. An asymmetric unit is therefore composed of 776 amino acids and has a molecular weight of 86233.70 Da.&lt;br /&gt;
&lt;br /&gt;
The A chain is made up of &amp;lt;scene name=&#039;82/829361/Helixalphachaina_asymunit/1&#039;&amp;gt;17 helices&amp;lt;/scene&amp;gt; (involving 221 residues) and &amp;lt;scene name=&#039;82/829361/Betasheetchaina_asymunit/1&#039;&amp;gt;14 beta-sheets&amp;lt;/scene&amp;gt; (61 residues).&lt;br /&gt;
Chain B is formed of &amp;lt;scene name=&#039;82/829361/Helixchainb_asymunit/1&#039;&amp;gt;17 helices&amp;lt;/scene&amp;gt; (involving 218 residues) and &amp;lt;scene name=&#039;82/829361/Betasheetchainb_asymunit/1&#039;&amp;gt;14 beta-sheets&amp;lt;/scene&amp;gt; (62 residues). &lt;br /&gt;
&lt;br /&gt;
==Tertiary structures==&lt;br /&gt;
==Enzymatic reaction==&lt;br /&gt;
&lt;br /&gt;
[[Enzyme accepted name]]: Short-chain acyl-CoA dehydrogenase&lt;br /&gt;
&lt;br /&gt;
[[Other names]]:Butanoyl-CoA dehydrogenase, Butyryl dehydrogenase, Short-chain acyl CoA dehydrogenase, Unsatured acyl-CoA reductase.&lt;br /&gt;
&lt;br /&gt;
[[Enzyme class]]: E.C.1.3.8.1[https://enzyme.expasy.org/EC/1.3.8.1]&lt;br /&gt;
&lt;br /&gt;
[[Substrate]]: A short-chain acyl CoA &lt;br /&gt;
&lt;br /&gt;
[[Prosthetic group]]: 1 electron-transfer flavoprotein such as FDA, for every Subunits &lt;br /&gt;
&lt;br /&gt;
[[Products]]: a short-chain trans-2,3-dehydroacyl-CoA + reduced electron-transfer flavoprotein&lt;br /&gt;
&lt;br /&gt;
[[Pathways]]: Fatty acid degradation&lt;br /&gt;
&lt;br /&gt;
[[Other information]]:&lt;br /&gt;
&lt;br /&gt;
The enzyme from beef liver can accept acyl-chain lengths from 3 to 8 carbon atoms. From different organism the range can vary so we ignore if M.tuberculosis gets the same lengths resolution.&lt;br /&gt;
&lt;br /&gt;
The highest activity reported for beef liver enzyme was for substrates with 4 and 5 carbon acyl-chain lengths.&lt;br /&gt;
&lt;br /&gt;
==4IV6 as a research tool==&lt;br /&gt;
&lt;br /&gt;
4iv6 which belong to &#039;&#039;Mycobacterium tuberculosis&#039;&#039; was studied with other protein homolog.&lt;br /&gt;
They were chosen to be studied as potential TB-Drugs target&lt;br /&gt;
Studies have been made on homolog similarities aimed on their active site because with the knowledges of many homolog active site structure and how they work, we can design a inhibitor of those enzyme which can stop essential reaction and reduce or stop &#039;&#039;M.tuberculosis&#039;&#039; infection.&lt;br /&gt;
This strategy is called an « Homolog-rescue strategy ».&lt;br /&gt;
This strategy can be generalized for other drug target for other diseases.&lt;br /&gt;
&lt;br /&gt;
&lt;br /&gt;
== Structural highlights ==&lt;br /&gt;
&amp;lt;scene name=&#039;82/829361/Biological_unit/1&#039;&amp;gt;Biological unit&amp;lt;/scene&amp;gt;&lt;br /&gt;
&lt;br /&gt;
&amp;lt;scene name=&#039;82/829361/Asymetrical_unit/2&#039;&amp;gt;Asymetrical unit&amp;lt;/scene&amp;gt; :Light Grey:1st sub-unit, Light green:2nd sub-unit, Blue and red:FDA &lt;br /&gt;
&lt;br /&gt;
&amp;lt;scene name=&#039;82/829361/Secondary_structure/1&#039;&amp;gt;Secondary structure&amp;lt;/scene&amp;gt; : Red: helix alpha, Blue:FDA, Yellow: Beta sheet  &lt;br /&gt;
&lt;br /&gt;
&amp;lt;scene name=&#039;82/829361/Hydrophobic/1&#039;&amp;gt;Hydrophobic region&amp;lt;/scene&amp;gt; : Green: FDA, Purple: Polar region, Light grey: Hydrophobic region &lt;br /&gt;
&lt;br /&gt;
&amp;lt;/StructureSection&amp;gt;&lt;br /&gt;
== References ==&lt;br /&gt;
&amp;lt;references/&amp;gt;&lt;/div&gt;</summary>
		<author><name>Appoline Dubois</name></author>
	</entry>
	<entry>
		<id>https://proteopedia.org/index.php?title=Sandbox_Reserved_1108&amp;diff=3143147</id>
		<title>Sandbox Reserved 1108</title>
		<link rel="alternate" type="text/html" href="https://proteopedia.org/index.php?title=Sandbox_Reserved_1108&amp;diff=3143147"/>
		<updated>2020-01-14T18:04:56Z</updated>

		<summary type="html">&lt;p&gt;Appoline Dubois: &lt;/p&gt;
&lt;hr /&gt;
&lt;div&gt;{{Sandbox_ESBS_2019}}&amp;lt;!-- PLEASE ADD YOUR CONTENT BELOW HERE --&amp;gt;&lt;br /&gt;
==Your Heading Here (maybe something like &#039;Structure&#039;)==&lt;br /&gt;
&amp;lt;StructureSection load=&#039;1stp&#039; size=&#039;340&#039; side=&#039;right&#039; caption=&#039;Caption for this structure&#039; scene=&#039;&#039;&amp;gt;&lt;br /&gt;
This is a default text for your page &#039;&#039;&#039;&#039;&#039;&#039;. Click above on &#039;&#039;&#039;edit this page&#039;&#039;&#039; to modify. Be careful with the &amp;amp;lt; and &amp;amp;gt; signs.&lt;br /&gt;
You may include any references to papers as in: the use of JSmol in Proteopedia &amp;lt;ref&amp;gt;DOI 10.1002/ijch.201300024&amp;lt;/ref&amp;gt; or to the article describing Jmol &amp;lt;ref&amp;gt;PMID:21638687&amp;lt;/ref&amp;gt; to the rescue.&lt;br /&gt;
&lt;br /&gt;
== Function ==&lt;br /&gt;
==Primary and Secondary structure&amp;lt;ref&amp;gt;http://www.rcsb.org/structure/4IV6&amp;lt;/ref&amp;gt;==&lt;br /&gt;
&lt;br /&gt;
Isovaleryl-CoA dehydrogenase is the assembly of &#039;&#039;&#039;&amp;lt;scene name=&#039;82/829361/2asymunit/1&#039;&amp;gt;two asymmetric units&amp;lt;/scene&amp;gt;&#039;&#039;&#039; each composed of &#039;&#039;&#039;two chains &amp;lt;scene name=&#039;82/829361/Chainea_asymunit/2&#039;&amp;gt;A&amp;lt;/scene&amp;gt; and &amp;lt;scene name=&#039;82/829361/Chaineb_asymunit/1&#039;&amp;gt;B&amp;lt;/scene&amp;gt;&#039;&#039;&#039; linked by a &amp;lt;scene name=&#039;82/829361/Ligand_asymunit/1&#039;&amp;gt;ligand&amp;lt;/scene&amp;gt; (Dihydroflavine-Adenine Dinucleotide also known as  	 [https://pubchem.ncbi.nlm.nih.gov/compound/Dihydroflavine-adenine-dinucleotide FADH2] ). Each of the two chains A and B are composed of 388 amino acids. An asymmetric unit is therefore composed of 776 amino acids and has a molecular weight of 86233.70 Da.&lt;br /&gt;
&lt;br /&gt;
The A chain is made up of &amp;lt;scene name=&#039;82/829361/Helixalphachaina_asymunit/1&#039;&amp;gt;17 helices&amp;lt;/scene&amp;gt; (involving 221 residues) and &amp;lt;scene name=&#039;82/829361/Betasheetchaina_asymunit/1&#039;&amp;gt;14 beta-sheets&amp;lt;/scene&amp;gt; (61 residues).&lt;br /&gt;
Chain B is formed of &amp;lt;scene name=&#039;82/829361/Helixchainb_asymunit/1&#039;&amp;gt;17 helices&amp;lt;/scene&amp;gt; (involving 218 residues) and &amp;lt;scene name=&#039;82/829361/Betasheetchainb_asymunit/1&#039;&amp;gt;14 beta-sheets&amp;lt;/scene&amp;gt; (62 residues). &lt;br /&gt;
&lt;br /&gt;
==Tertiary structures==&lt;br /&gt;
==Enzymatic reaction==&lt;br /&gt;
&lt;br /&gt;
[[Enzyme accepted name]]: Short-chain acyl-CoA dehydrogenase&lt;br /&gt;
&lt;br /&gt;
[[Other names]]:Butanoyl-CoA dehydrogenase, Butyryl dehydrogenase, Short-chain acyl CoA dehydrogenase, Unsatured acyl-CoA reductase.&lt;br /&gt;
&lt;br /&gt;
[[Enzyme class]]: E.C.1.3.8.1[https://enzyme.expasy.org/EC/1.3.8.1]&lt;br /&gt;
&lt;br /&gt;
[[Substrate]]: A short-chain acyl CoA &lt;br /&gt;
&lt;br /&gt;
[[Prosthetic group]]: 1 electron-transfer flavoprotein such as FDA, for every Subunits &lt;br /&gt;
&lt;br /&gt;
[[Products]]: a short-chain trans-2,3-dehydroacyl-CoA + reduced electron-transfer flavoprotein&lt;br /&gt;
&lt;br /&gt;
[[Pathways]]: Fatty acid degradation&lt;br /&gt;
&lt;br /&gt;
[[Other information]]:&lt;br /&gt;
&lt;br /&gt;
The enzyme from beef liver can accept acyl-chain lengths from 3 to 8 carbon atoms. From different organism the range can vary so we ignore if M.tuberculosis gets the same lengths resolution.&lt;br /&gt;
&lt;br /&gt;
The highest activity reported for beef liver enzyme was for substrates with 4 and 5 carbon acyl-chain lengths.&lt;br /&gt;
&lt;br /&gt;
==4IV6 as a research tool==&lt;br /&gt;
&lt;br /&gt;
4iv6 which belong to &#039;&#039;Mycobacterium tuberculosis&#039;&#039; was studied with other protein homolog.&lt;br /&gt;
They were chosen to be studied as potential TB-Drugs target&lt;br /&gt;
Studies have been made on homolog similarities aimed on their active site because with the knowledges of many homolog active site structure and how they work, we can design a inhibitor of those enzyme which can stop essential reaction and reduce or stop &#039;&#039;M.tuberculosis&#039;&#039; infection.&lt;br /&gt;
This strategy is called an « Homolog-rescue strategy ».&lt;br /&gt;
This strategy can be generalized for other drug target for other diseases.&lt;br /&gt;
&lt;br /&gt;
&lt;br /&gt;
== Structural highlights ==&lt;br /&gt;
&amp;lt;scene name=&#039;82/829361/Biological_unit/1&#039;&amp;gt;Biological unit&amp;lt;/scene&amp;gt;&lt;br /&gt;
&lt;br /&gt;
&amp;lt;scene name=&#039;82/829361/Asymetrical_unit/2&#039;&amp;gt;Asymetrical unit&amp;lt;/scene&amp;gt; :Light Grey:1st sub-unit, Light green:2nd sub-unit, Blue and red:FDA &lt;br /&gt;
&lt;br /&gt;
&amp;lt;scene name=&#039;82/829361/Secondary_structure/1&#039;&amp;gt;Secondary structure&amp;lt;/scene&amp;gt; : Red: helix alpha, Blue:FDA, Yellow: Beta sheet  &lt;br /&gt;
&lt;br /&gt;
&amp;lt;scene name=&#039;82/829361/Hydrophobic/1&#039;&amp;gt;Hydrophobic region&amp;lt;/scene&amp;gt; : Green: FDA, Purple: Polar region, Light grey: Hydrophobic region &lt;br /&gt;
&lt;br /&gt;
&amp;lt;/StructureSection&amp;gt;&lt;br /&gt;
== References ==&lt;br /&gt;
&amp;lt;references/&amp;gt;&lt;/div&gt;</summary>
		<author><name>Appoline Dubois</name></author>
	</entry>
	<entry>
		<id>https://proteopedia.org/index.php?title=Sandbox_Reserved_1108&amp;diff=3143145</id>
		<title>Sandbox Reserved 1108</title>
		<link rel="alternate" type="text/html" href="https://proteopedia.org/index.php?title=Sandbox_Reserved_1108&amp;diff=3143145"/>
		<updated>2020-01-14T18:02:04Z</updated>

		<summary type="html">&lt;p&gt;Appoline Dubois: &lt;/p&gt;
&lt;hr /&gt;
&lt;div&gt;{{Sandbox_ESBS_2019}}&amp;lt;!-- PLEASE ADD YOUR CONTENT BELOW HERE --&amp;gt;&lt;br /&gt;
==Your Heading Here (maybe something like &#039;Structure&#039;)==&lt;br /&gt;
&amp;lt;StructureSection load=&#039;1stp&#039; size=&#039;340&#039; side=&#039;right&#039; caption=&#039;Caption for this structure&#039; scene=&#039;&#039;&amp;gt;&lt;br /&gt;
This is a default text for your page &#039;&#039;&#039;&#039;&#039;&#039;. Click above on &#039;&#039;&#039;edit this page&#039;&#039;&#039; to modify. Be careful with the &amp;amp;lt; and &amp;amp;gt; signs.&lt;br /&gt;
You may include any references to papers as in: the use of JSmol in Proteopedia &amp;lt;ref&amp;gt;DOI 10.1002/ijch.201300024&amp;lt;/ref&amp;gt; or to the article describing Jmol &amp;lt;ref&amp;gt;PMID:21638687&amp;lt;/ref&amp;gt; to the rescue.&lt;br /&gt;
&lt;br /&gt;
== Function ==&lt;br /&gt;
==Primary and Secondary structure==&lt;br /&gt;
&lt;br /&gt;
Isovaleryl-CoA dehydrogenase is the assembly of &#039;&#039;&#039;&amp;lt;scene name=&#039;82/829361/2asymunit/1&#039;&amp;gt;two asymmetric units&amp;lt;/scene&amp;gt;&#039;&#039;&#039; each composed of &#039;&#039;&#039;two chains &amp;lt;scene name=&#039;82/829361/Chainea_asymunit/2&#039;&amp;gt;A&amp;lt;/scene&amp;gt; and &amp;lt;scene name=&#039;82/829361/Chaineb_asymunit/1&#039;&amp;gt;B&amp;lt;/scene&amp;gt;&#039;&#039;&#039; linked by a &amp;lt;scene name=&#039;82/829361/Ligand_asymunit/1&#039;&amp;gt;ligand&amp;lt;/scene&amp;gt; (Dihydroflavine-Adenine Dinucleotide also known as  	 [https://pubchem.ncbi.nlm.nih.gov/compound/Dihydroflavine-adenine-dinucleotide FADH2] ). Each of the two chains A and B are composed of 388 amino acids. An asymmetric unit is therefore composed of 776 amino acids and has a molecular weight of 86233.70 Da.&lt;br /&gt;
&lt;br /&gt;
The A chain is made up of &amp;lt;scene name=&#039;82/829361/Helixalphachaina_asymunit/1&#039;&amp;gt;17 helices&amp;lt;/scene&amp;gt; (involving 221 residues) and &amp;lt;scene name=&#039;82/829361/Betasheetchaina_asymunit/1&#039;&amp;gt;14 beta-sheets&amp;lt;/scene&amp;gt; (61 residues).&lt;br /&gt;
Chain B is formed of &amp;lt;scene name=&#039;82/829361/Helixchainb_asymunit/1&#039;&amp;gt;17 helices&amp;lt;/scene&amp;gt; (involving 218 residues) and &amp;lt;scene name=&#039;82/829361/Betasheetchainb_asymunit/1&#039;&amp;gt;14 beta-sheets&amp;lt;/scene&amp;gt; (62 residues). &lt;br /&gt;
&lt;br /&gt;
==Tertiary structures==&lt;br /&gt;
==Enzymatic reaction==&lt;br /&gt;
&lt;br /&gt;
[[Enzyme accepted name]]: Short-chain acyl-CoA dehydrogenase&lt;br /&gt;
&lt;br /&gt;
[[Other names]]:Butanoyl-CoA dehydrogenase, Butyryl dehydrogenase, Short-chain acyl CoA dehydrogenase, Unsatured acyl-CoA reductase.&lt;br /&gt;
&lt;br /&gt;
[[Enzyme class]]: E.C.1.3.8.1[https://enzyme.expasy.org/EC/1.3.8.1]&lt;br /&gt;
&lt;br /&gt;
[[Substrate]]: A short-chain acyl CoA &lt;br /&gt;
&lt;br /&gt;
[[Prosthetic group]]: 1 electron-transfer flavoprotein such as FDA, for every Subunits &lt;br /&gt;
&lt;br /&gt;
[[Products]]: a short-chain trans-2,3-dehydroacyl-CoA + reduced electron-transfer flavoprotein&lt;br /&gt;
&lt;br /&gt;
[[Pathways]]: Fatty acid degradation&lt;br /&gt;
&lt;br /&gt;
[[Other information]]:&lt;br /&gt;
&lt;br /&gt;
The enzyme from beef liver can accept acyl-chain lengths from 3 to 8 carbon atoms. From different organism the range can vary so we ignore if M.tuberculosis gets the same lengths resolution.&lt;br /&gt;
&lt;br /&gt;
The highest activity reported for beef liver enzyme was for substrates with 4 and 5 carbon acyl-chain lengths.&lt;br /&gt;
&lt;br /&gt;
==4IV6 as a research tool==&lt;br /&gt;
&lt;br /&gt;
4iv6 which belong to &#039;&#039;Mycobacterium tuberculosis&#039;&#039; was studied with other protein homolog.&lt;br /&gt;
They were chosen to be studied as potential TB-Drugs target&lt;br /&gt;
Studies have been made on homolog similarities aimed on their active site because with the knowledges of many homolog active site structure and how they work, we can design a inhibitor of those enzyme which can stop essential reaction and reduce or stop &#039;&#039;M.tuberculosis&#039;&#039; infection.&lt;br /&gt;
This strategy is called an « Homolog-rescue strategy ».&lt;br /&gt;
This strategy can be generalized for other drug target for other diseases.&lt;br /&gt;
&lt;br /&gt;
&lt;br /&gt;
== Structural highlights ==&lt;br /&gt;
&amp;lt;scene name=&#039;82/829361/Biological_unit/1&#039;&amp;gt;Biological unit&amp;lt;/scene&amp;gt;&lt;br /&gt;
&lt;br /&gt;
&amp;lt;scene name=&#039;82/829361/Asymetrical_unit/2&#039;&amp;gt;Asymetrical unit&amp;lt;/scene&amp;gt; :Light Grey:1st sub-unit, Light green:2nd sub-unit, Blue and red:FDA &lt;br /&gt;
&lt;br /&gt;
&amp;lt;scene name=&#039;82/829361/Secondary_structure/1&#039;&amp;gt;Secondary structure&amp;lt;/scene&amp;gt; : Red: helix alpha, Blue:FDA, Yellow: Beta sheet  &lt;br /&gt;
&lt;br /&gt;
&amp;lt;scene name=&#039;82/829361/Hydrophobic/1&#039;&amp;gt;Hydrophobic region&amp;lt;/scene&amp;gt; : Green: FDA, Purple: Polar region, Light grey: Hydrophobic region &lt;br /&gt;
&lt;br /&gt;
&amp;lt;/StructureSection&amp;gt;&lt;br /&gt;
== References ==&lt;br /&gt;
&amp;lt;references/&amp;gt;&lt;/div&gt;</summary>
		<author><name>Appoline Dubois</name></author>
	</entry>
	<entry>
		<id>https://proteopedia.org/index.php?title=Sandbox_Reserved_1108&amp;diff=3143144</id>
		<title>Sandbox Reserved 1108</title>
		<link rel="alternate" type="text/html" href="https://proteopedia.org/index.php?title=Sandbox_Reserved_1108&amp;diff=3143144"/>
		<updated>2020-01-14T18:00:58Z</updated>

		<summary type="html">&lt;p&gt;Appoline Dubois: &lt;/p&gt;
&lt;hr /&gt;
&lt;div&gt;{{Sandbox_ESBS_2019}}&amp;lt;!-- PLEASE ADD YOUR CONTENT BELOW HERE --&amp;gt;&lt;br /&gt;
==Your Heading Here (maybe something like &#039;Structure&#039;)==&lt;br /&gt;
&amp;lt;StructureSection load=&#039;1stp&#039; size=&#039;340&#039; side=&#039;right&#039; caption=&#039;Caption for this structure&#039; scene=&#039;&#039;&amp;gt;&lt;br /&gt;
This is a default text for your page &#039;&#039;&#039;&#039;&#039;&#039;. Click above on &#039;&#039;&#039;edit this page&#039;&#039;&#039; to modify. Be careful with the &amp;amp;lt; and &amp;amp;gt; signs.&lt;br /&gt;
You may include any references to papers as in: the use of JSmol in Proteopedia &amp;lt;ref&amp;gt;DOI 10.1002/ijch.201300024&amp;lt;/ref&amp;gt; or to the article describing Jmol &amp;lt;ref&amp;gt;PMID:21638687&amp;lt;/ref&amp;gt; to the rescue.&lt;br /&gt;
&lt;br /&gt;
== Function ==&lt;br /&gt;
==Primary and Secondary structure==&lt;br /&gt;
&lt;br /&gt;
Isovaleryl-CoA dehydrogenase is the assembly of &#039;&#039;&#039;&amp;lt;scene name=&#039;82/829361/2asymunit/1&#039;&amp;gt;two asymmetric units&amp;lt;/scene&amp;gt;&#039;&#039;&#039; each composed of &#039;&#039;&#039;two chains &amp;lt;scene name=&#039;82/829361/Chainea_asymunit/2&#039;&amp;gt;A&amp;lt;/scene&amp;gt; and &amp;lt;scene name=&#039;82/829361/Chaineb_asymunit/1&#039;&amp;gt;B&amp;lt;/scene&amp;gt;&#039;&#039;&#039; linked by a &amp;lt;scene name=&#039;82/829361/Ligand_asymunit/1&#039;&amp;gt;ligand&amp;lt;/scene&amp;gt; (Dihydroflavine-Adenine Dinucleotide also known as  	&lt;br /&gt;
&lt;br /&gt;
[https://pubchem.ncbi.nlm.nih.gov/compound/Dihydroflavine-adenine-dinucleotide/ FADH2] ). Each of the two chains A and B are composed of 388 amino acids. An asymmetric unit is therefore composed of 776 amino acids and has a molecular weight of 86233.70 Da.&lt;br /&gt;
&lt;br /&gt;
The A chain is made up of &amp;lt;scene name=&#039;82/829361/Helixalphachaina_asymunit/1&#039;&amp;gt;17 helices&amp;lt;/scene&amp;gt; (involving 221 residues) and &amp;lt;scene name=&#039;82/829361/Betasheetchaina_asymunit/1&#039;&amp;gt;14 beta-sheets&amp;lt;/scene&amp;gt; (61 residues).&lt;br /&gt;
Chain B is formed of &amp;lt;scene name=&#039;82/829361/Helixchainb_asymunit/1&#039;&amp;gt;17 helices&amp;lt;/scene&amp;gt; (involving 218 residues) and &amp;lt;scene name=&#039;82/829361/Betasheetchainb_asymunit/1&#039;&amp;gt;14 beta-sheets&amp;lt;/scene&amp;gt; (62 residues). &lt;br /&gt;
&lt;br /&gt;
==Tertiary structures==&lt;br /&gt;
==Enzymatic reaction==&lt;br /&gt;
&lt;br /&gt;
[[Enzyme accepted name]]: Short-chain acyl-CoA dehydrogenase&lt;br /&gt;
&lt;br /&gt;
[[Other names]]:Butanoyl-CoA dehydrogenase, Butyryl dehydrogenase, Short-chain acyl CoA dehydrogenase, Unsatured acyl-CoA reductase.&lt;br /&gt;
&lt;br /&gt;
[[Enzyme class]]: E.C.1.3.8.1[https://enzyme.expasy.org/EC/1.3.8.1]&lt;br /&gt;
&lt;br /&gt;
[[Substrate]]: A short-chain acyl CoA &lt;br /&gt;
&lt;br /&gt;
[[Prosthetic group]]: 1 electron-transfer flavoprotein such as FDA, for every Subunits &lt;br /&gt;
&lt;br /&gt;
[[Products]]: a short-chain trans-2,3-dehydroacyl-CoA + reduced electron-transfer flavoprotein&lt;br /&gt;
&lt;br /&gt;
[[Pathways]]: Fatty acid degradation&lt;br /&gt;
&lt;br /&gt;
[[Other information]]:&lt;br /&gt;
&lt;br /&gt;
The enzyme from beef liver can accept acyl-chain lengths from 3 to 8 carbon atoms. From different organism the range can vary so we ignore if M.tuberculosis gets the same lengths resolution.&lt;br /&gt;
&lt;br /&gt;
The highest activity reported for beef liver enzyme was for substrates with 4 and 5 carbon acyl-chain lengths.&lt;br /&gt;
&lt;br /&gt;
==4IV6 as a research tool==&lt;br /&gt;
&lt;br /&gt;
4iv6 which belong to &#039;&#039;Mycobacterium tuberculosis&#039;&#039; was studied with other protein homolog.&lt;br /&gt;
They were chosen to be studied as potential TB-Drugs target&lt;br /&gt;
Studies have been made on homolog similarities aimed on their active site because with the knowledges of many homolog active site structure and how they work, we can design a inhibitor of those enzyme which can stop essential reaction and reduce or stop &#039;&#039;M.tuberculosis&#039;&#039; infection.&lt;br /&gt;
This strategy is called an « Homolog-rescue strategy ».&lt;br /&gt;
This strategy can be generalized for other drug target for other diseases.&lt;br /&gt;
&lt;br /&gt;
&lt;br /&gt;
== Structural highlights ==&lt;br /&gt;
&amp;lt;scene name=&#039;82/829361/Biological_unit/1&#039;&amp;gt;Biological unit&amp;lt;/scene&amp;gt;&lt;br /&gt;
&lt;br /&gt;
&amp;lt;scene name=&#039;82/829361/Asymetrical_unit/2&#039;&amp;gt;Asymetrical unit&amp;lt;/scene&amp;gt; :Light Grey:1st sub-unit, Light green:2nd sub-unit, Blue and red:FDA &lt;br /&gt;
&lt;br /&gt;
&amp;lt;scene name=&#039;82/829361/Secondary_structure/1&#039;&amp;gt;Secondary structure&amp;lt;/scene&amp;gt; : Red: helix alpha, Blue:FDA, Yellow: Beta sheet  &lt;br /&gt;
&lt;br /&gt;
&amp;lt;scene name=&#039;82/829361/Hydrophobic/1&#039;&amp;gt;Hydrophobic region&amp;lt;/scene&amp;gt; : Green: FDA, Purple: Polar region, Light grey: Hydrophobic region &lt;br /&gt;
&lt;br /&gt;
&amp;lt;/StructureSection&amp;gt;&lt;br /&gt;
== References ==&lt;br /&gt;
&amp;lt;references/&amp;gt;&lt;/div&gt;</summary>
		<author><name>Appoline Dubois</name></author>
	</entry>
	<entry>
		<id>https://proteopedia.org/index.php?title=Sandbox_Reserved_1108&amp;diff=3143140</id>
		<title>Sandbox Reserved 1108</title>
		<link rel="alternate" type="text/html" href="https://proteopedia.org/index.php?title=Sandbox_Reserved_1108&amp;diff=3143140"/>
		<updated>2020-01-14T17:56:05Z</updated>

		<summary type="html">&lt;p&gt;Appoline Dubois: &lt;/p&gt;
&lt;hr /&gt;
&lt;div&gt;{{Sandbox_ESBS_2019}}&amp;lt;!-- PLEASE ADD YOUR CONTENT BELOW HERE --&amp;gt;&lt;br /&gt;
==Your Heading Here (maybe something like &#039;Structure&#039;)==&lt;br /&gt;
&amp;lt;StructureSection load=&#039;1stp&#039; size=&#039;340&#039; side=&#039;right&#039; caption=&#039;Caption for this structure&#039; scene=&#039;&#039;&amp;gt;&lt;br /&gt;
This is a default text for your page &#039;&#039;&#039;&#039;&#039;&#039;. Click above on &#039;&#039;&#039;edit this page&#039;&#039;&#039; to modify. Be careful with the &amp;amp;lt; and &amp;amp;gt; signs.&lt;br /&gt;
You may include any references to papers as in: the use of JSmol in Proteopedia &amp;lt;ref&amp;gt;DOI 10.1002/ijch.201300024&amp;lt;/ref&amp;gt; or to the article describing Jmol &amp;lt;ref&amp;gt;PMID:21638687&amp;lt;/ref&amp;gt; to the rescue.&lt;br /&gt;
&lt;br /&gt;
== Function ==&lt;br /&gt;
==Primary and Secondary structure==&lt;br /&gt;
&lt;br /&gt;
Isovaleryl-CoA dehydrogenase is the assembly of &#039;&#039;&#039;&amp;lt;scene name=&#039;82/829361/2asymunit/1&#039;&amp;gt;two asymmetric units&amp;lt;/scene&amp;gt;&#039;&#039;&#039; each composed of &#039;&#039;&#039;two chains &amp;lt;scene name=&#039;82/829361/Chainea_asymunit/2&#039;&amp;gt;A&amp;lt;/scene&amp;gt; and &amp;lt;scene name=&#039;82/829361/Chaineb_asymunit/1&#039;&amp;gt;B&amp;lt;/scene&amp;gt;&#039;&#039;&#039; linked by a &amp;lt;scene name=&#039;82/829361/Ligand_asymunit/1&#039;&amp;gt;ligand&amp;lt;/scene&amp;gt; (Dihydroflavine-Adenine Dinucleotide also known as FADH2). Each of the two chains A and B are composed of 388 amino acids. An asymmetric unit is therefore composed of 776 amino acids and has a molecular weight of 86233.70 Da.&lt;br /&gt;
&lt;br /&gt;
The A chain is made up of &amp;lt;scene name=&#039;82/829361/Helixalphachaina_asymunit/1&#039;&amp;gt;17 helices&amp;lt;/scene&amp;gt; (involving 221 residues) and &amp;lt;scene name=&#039;82/829361/Betasheetchaina_asymunit/1&#039;&amp;gt;14 beta-sheets&amp;lt;/scene&amp;gt; (61 residues).&lt;br /&gt;
Chain B is formed of &amp;lt;scene name=&#039;82/829361/Helixchainb_asymunit/1&#039;&amp;gt;17 helices&amp;lt;/scene&amp;gt; (involving 218 residues) and &amp;lt;scene name=&#039;82/829361/Betasheetchainb_asymunit/1&#039;&amp;gt;14 beta-sheets&amp;lt;/scene&amp;gt; (62 residues). &lt;br /&gt;
&lt;br /&gt;
==Tertiary structures==&lt;br /&gt;
==Enzymatic reaction==&lt;br /&gt;
&lt;br /&gt;
[[Enzyme accepted name]]: Short-chain acyl-CoA dehydrogenase&lt;br /&gt;
&lt;br /&gt;
[[Other names]]:Butanoyl-CoA dehydrogenase, Butyryl dehydrogenase, Short-chain acyl CoA dehydrogenase, Unsatured acyl-CoA reductase.&lt;br /&gt;
&lt;br /&gt;
[[Enzyme class]]: E.C.1.3.8.1[https://enzyme.expasy.org/EC/1.3.8.1]&lt;br /&gt;
&lt;br /&gt;
[[Substrate]]: A short-chain acyl CoA &lt;br /&gt;
&lt;br /&gt;
[[Prosthetic group]]: 1 electron-transfer flavoprotein such as FDA, for every Subunits &lt;br /&gt;
&lt;br /&gt;
[[Products]]: a short-chain trans-2,3-dehydroacyl-CoA + reduced electron-transfer flavoprotein&lt;br /&gt;
&lt;br /&gt;
[[Pathways]]: Fatty acid degradation&lt;br /&gt;
&lt;br /&gt;
[[Other information]]:&lt;br /&gt;
&lt;br /&gt;
The enzyme from beef liver can accept acyl-chain lengths from 3 to 8 carbon atoms. From different organism the range can vary so we ignore if M.tuberculosis gets the same lengths resolution.&lt;br /&gt;
&lt;br /&gt;
The highest activity reported for beef liver enzyme was for substrates with 4 and 5 carbon acyl-chain lengths.&lt;br /&gt;
&lt;br /&gt;
==4IV6 as a research tool==&lt;br /&gt;
&lt;br /&gt;
4iv6 which belong to &#039;&#039;Mycobacterium tuberculosis&#039;&#039; was studied with other protein homolog.&lt;br /&gt;
They were chosen to be studied as potential TB-Drugs target&lt;br /&gt;
Studies have been made on homolog similarities aimed on their active site because with the knowledges of many homolog active site structure and how they work, we can design a inhibitor of those enzyme which can stop essential reaction and reduce or stop &#039;&#039;M.tuberculosis&#039;&#039; infection.&lt;br /&gt;
This strategy is called an « Homolog-rescue strategy ».&lt;br /&gt;
This strategy can be generalized for other drug target for other diseases.&lt;br /&gt;
&lt;br /&gt;
&lt;br /&gt;
== Structural highlights ==&lt;br /&gt;
&amp;lt;scene name=&#039;82/829361/Biological_unit/1&#039;&amp;gt;Biological unit&amp;lt;/scene&amp;gt;&lt;br /&gt;
&lt;br /&gt;
&amp;lt;scene name=&#039;82/829361/Asymetrical_unit/2&#039;&amp;gt;Asymetrical unit&amp;lt;/scene&amp;gt; :Light Grey:1st sub-unit, Light green:2nd sub-unit, Blue and red:FDA &lt;br /&gt;
&lt;br /&gt;
&amp;lt;scene name=&#039;82/829361/Secondary_structure/1&#039;&amp;gt;Secondary structure&amp;lt;/scene&amp;gt; : Red: helix alpha, Blue:FDA, Yellow: Beta sheet  &lt;br /&gt;
&lt;br /&gt;
&amp;lt;scene name=&#039;82/829361/Hydrophobic/1&#039;&amp;gt;Hydrophobic region&amp;lt;/scene&amp;gt; : Green: FDA, Purple: Polar region, Light grey: Hydrophobic region &lt;br /&gt;
&lt;br /&gt;
&amp;lt;/StructureSection&amp;gt;&lt;br /&gt;
== References ==&lt;br /&gt;
&amp;lt;references/&amp;gt;&lt;/div&gt;</summary>
		<author><name>Appoline Dubois</name></author>
	</entry>
	<entry>
		<id>https://proteopedia.org/index.php?title=Sandbox_Reserved_1108&amp;diff=3143132</id>
		<title>Sandbox Reserved 1108</title>
		<link rel="alternate" type="text/html" href="https://proteopedia.org/index.php?title=Sandbox_Reserved_1108&amp;diff=3143132"/>
		<updated>2020-01-14T17:50:13Z</updated>

		<summary type="html">&lt;p&gt;Appoline Dubois: &lt;/p&gt;
&lt;hr /&gt;
&lt;div&gt;{{Sandbox_ESBS_2019}}&amp;lt;!-- PLEASE ADD YOUR CONTENT BELOW HERE --&amp;gt;&lt;br /&gt;
==Your Heading Here (maybe something like &#039;Structure&#039;)==&lt;br /&gt;
&amp;lt;StructureSection load=&#039;1stp&#039; size=&#039;340&#039; side=&#039;right&#039; caption=&#039;Caption for this structure&#039; scene=&#039;&#039;&amp;gt;&lt;br /&gt;
This is a default text for your page &#039;&#039;&#039;&#039;&#039;&#039;. Click above on &#039;&#039;&#039;edit this page&#039;&#039;&#039; to modify. Be careful with the &amp;amp;lt; and &amp;amp;gt; signs.&lt;br /&gt;
You may include any references to papers as in: the use of JSmol in Proteopedia &amp;lt;ref&amp;gt;DOI 10.1002/ijch.201300024&amp;lt;/ref&amp;gt; or to the article describing Jmol &amp;lt;ref&amp;gt;PMID:21638687&amp;lt;/ref&amp;gt; to the rescue.&lt;br /&gt;
&lt;br /&gt;
== Function ==&lt;br /&gt;
==Primary and Secondary structure==&lt;br /&gt;
&lt;br /&gt;
Isovaleryl-CoA dehydrogenase is the assembly of &#039;&#039;&#039;&amp;lt;scene name=&#039;82/829361/2asymunit/1&#039;&amp;gt;two asymmetric units&amp;lt;/scene&amp;gt;&#039;&#039;&#039; each composed of &#039;&#039;&#039;two chains &amp;lt;scene name=&#039;82/829361/Chainea_asymunit/2&#039;&amp;gt;A&amp;lt;/scene&amp;gt; and &amp;lt;scene name=&#039;82/829361/Chaineb_asymunit/1&#039;&amp;gt;B&amp;lt;/scene&amp;gt;&#039;&#039;&#039; linked by a &amp;lt;scene name=&#039;82/829361/Ligand_asymunit/1&#039;&amp;gt;ligand&amp;lt;/scene&amp;gt; (Dihydroflavine-Adenine Dinucleotide). Each of the two chains A and B are composed of 388 amino acids. An asymmetric unit is therefore composed of 776 amino acids and has a molecular weight of 86233.70 Da.&lt;br /&gt;
&lt;br /&gt;
The A chain is made up of &amp;lt;scene name=&#039;82/829361/Helixalphachaina_asymunit/1&#039;&amp;gt;17 helices&amp;lt;/scene&amp;gt; (involving 221 residues) and &amp;lt;scene name=&#039;82/829361/Betasheetchaina_asymunit/1&#039;&amp;gt;14 beta-sheets&amp;lt;/scene&amp;gt; (61 residues).&lt;br /&gt;
Chain B is formed of &amp;lt;scene name=&#039;82/829361/Helixchainb_asymunit/1&#039;&amp;gt;17 helices&amp;lt;/scene&amp;gt; (involving 218 residues) and &amp;lt;scene name=&#039;82/829361/Betasheetchainb_asymunit/1&#039;&amp;gt;14 beta-sheets&amp;lt;/scene&amp;gt; (62 residues). &lt;br /&gt;
&lt;br /&gt;
==Tertiary structures==&lt;br /&gt;
==Enzymatic reaction==&lt;br /&gt;
&lt;br /&gt;
[[Enzyme accepted name]]: Short-chain acyl-CoA dehydrogenase&lt;br /&gt;
&lt;br /&gt;
[[Other names]]:Butanoyl-CoA dehydrogenase, Butyryl dehydrogenase, Short-chain acyl CoA dehydrogenase, Unsatured acyl-CoA reductase.&lt;br /&gt;
&lt;br /&gt;
[[Enzyme class]]: E.C.1.3.8.1[https://enzyme.expasy.org/EC/1.3.8.1]&lt;br /&gt;
&lt;br /&gt;
[[Substrate]]: A short-chain acyl CoA &lt;br /&gt;
&lt;br /&gt;
[[Prosthetic group]]: 1 electron-transfer flavoprotein such as FDA, for every Subunits &lt;br /&gt;
&lt;br /&gt;
[[Products]]: a short-chain trans-2,3-dehydroacyl-CoA + reduced electron-transfer flavoprotein&lt;br /&gt;
&lt;br /&gt;
[[Pathways]]: Fatty acid degradation&lt;br /&gt;
&lt;br /&gt;
[[Other information]]:&lt;br /&gt;
&lt;br /&gt;
The enzyme from beef liver can accept acyl-chain lengths from 3 to 8 carbon atoms. From different organism the range can vary so we ignore if M.tuberculosis gets the same lengths resolution.&lt;br /&gt;
&lt;br /&gt;
The highest activity reported for beef liver enzyme was for substrates with 4 and 5 carbon acyl-chain lengths.&lt;br /&gt;
&lt;br /&gt;
==4IV6 as a research tool==&lt;br /&gt;
&lt;br /&gt;
4iv6 which belong to &#039;&#039;Mycobacterium tuberculosis&#039;&#039; was studied with other protein homolog.&lt;br /&gt;
They were chosen to be studied as potential TB-Drugs target&lt;br /&gt;
Studies have been made on homolog similarities aimed on their active site because with the knowledges of many homolog active site structure and how they work, we can design a inhibitor of those enzyme which can stop essential reaction and reduce or stop &#039;&#039;M.tuberculosis&#039;&#039; infection.&lt;br /&gt;
This strategy is called an « Homolog-rescue strategy ».&lt;br /&gt;
This strategy can be generalized for other drug target for other diseases.&lt;br /&gt;
&lt;br /&gt;
&lt;br /&gt;
== Structural highlights ==&lt;br /&gt;
&amp;lt;scene name=&#039;82/829361/Biological_unit/1&#039;&amp;gt;Biological unit&amp;lt;/scene&amp;gt;&lt;br /&gt;
&lt;br /&gt;
&amp;lt;scene name=&#039;82/829361/Asymetrical_unit/2&#039;&amp;gt;Asymetrical unit&amp;lt;/scene&amp;gt; :Light Grey:1st sub-unit, Light green:2nd sub-unit, Blue and red:FDA &lt;br /&gt;
&lt;br /&gt;
&amp;lt;scene name=&#039;82/829361/Secondary_structure/1&#039;&amp;gt;Secondary structure&amp;lt;/scene&amp;gt; : Red: helix alpha, Blue:FDA, Yellow: Beta sheet  &lt;br /&gt;
&lt;br /&gt;
&amp;lt;scene name=&#039;82/829361/Hydrophobic/1&#039;&amp;gt;Hydrophobic region&amp;lt;/scene&amp;gt; : Green: FDA, Purple: Polar region, Light grey: Hydrophobic region &lt;br /&gt;
&lt;br /&gt;
&amp;lt;/StructureSection&amp;gt;&lt;br /&gt;
== References ==&lt;br /&gt;
&amp;lt;references/&amp;gt;&lt;/div&gt;</summary>
		<author><name>Appoline Dubois</name></author>
	</entry>
	<entry>
		<id>https://proteopedia.org/index.php?title=Sandbox_Reserved_1108&amp;diff=3143123</id>
		<title>Sandbox Reserved 1108</title>
		<link rel="alternate" type="text/html" href="https://proteopedia.org/index.php?title=Sandbox_Reserved_1108&amp;diff=3143123"/>
		<updated>2020-01-14T17:46:45Z</updated>

		<summary type="html">&lt;p&gt;Appoline Dubois: &lt;/p&gt;
&lt;hr /&gt;
&lt;div&gt;{{Sandbox_ESBS_2019}}&amp;lt;!-- PLEASE ADD YOUR CONTENT BELOW HERE --&amp;gt;&lt;br /&gt;
==Your Heading Here (maybe something like &#039;Structure&#039;)==&lt;br /&gt;
&amp;lt;StructureSection load=&#039;1stp&#039; size=&#039;340&#039; side=&#039;right&#039; caption=&#039;Caption for this structure&#039; scene=&#039;&#039;&amp;gt;&lt;br /&gt;
This is a default text for your page &#039;&#039;&#039;&#039;&#039;&#039;. Click above on &#039;&#039;&#039;edit this page&#039;&#039;&#039; to modify. Be careful with the &amp;amp;lt; and &amp;amp;gt; signs.&lt;br /&gt;
You may include any references to papers as in: the use of JSmol in Proteopedia &amp;lt;ref&amp;gt;DOI 10.1002/ijch.201300024&amp;lt;/ref&amp;gt; or to the article describing Jmol &amp;lt;ref&amp;gt;PMID:21638687&amp;lt;/ref&amp;gt; to the rescue.&lt;br /&gt;
&lt;br /&gt;
== Function ==&lt;br /&gt;
==Primary and Secondary structure==&lt;br /&gt;
&lt;br /&gt;
Isovaleryl-CoA dehydrogenase is the assembly of &#039;&#039;&#039;&amp;lt;scene name=&#039;82/829361/2asymunit/1&#039;&amp;gt;two asymmetric units&amp;lt;/scene&amp;gt;&#039;&#039;&#039; each composed of &#039;&#039;&#039;two chains &amp;lt;scene name=&#039;82/829361/Chainea_asymunit/2&#039;&amp;gt;A&amp;lt;/scene&amp;gt; and &amp;lt;scene name=&#039;82/829361/Chaineb_asymunit/1&#039;&amp;gt;B&amp;lt;/scene&amp;gt;&#039;&#039;&#039; linked by a &amp;lt;scene name=&#039;82/829361/Ligand_asymunit/1&#039;&amp;gt;ligand&amp;lt;/scene&amp;gt; (Dihydroflavine-Adenine Dinucleotide). Each of the two chains A and B are composed of 388 amino acids. An asymmetric unit is therefore composed of 776 amino acids and has a molecular weight of 86233.70 Da.&lt;br /&gt;
&lt;br /&gt;
The A chain is made up of &amp;lt;scene name=&#039;82/829361/Helixalphachaina_asymunit/1&#039;&amp;gt;17 helices&amp;lt;/scene&amp;gt; (involving 221 residues) and &amp;lt;scene name=&#039;82/829361/Betasheetchaina_asymunit/1&#039;&amp;gt;14 beta-sheets&amp;lt;/scene&amp;gt; (61 residues).&lt;br /&gt;
Chain B is formed of 17 helices (involving 218 residues) and 14 beta-sheets (62 residues). &lt;br /&gt;
&lt;br /&gt;
==Tertiary structures==&lt;br /&gt;
==Enzymatic reaction==&lt;br /&gt;
&lt;br /&gt;
[[Enzyme accepted name]]: Short-chain acyl-CoA dehydrogenase&lt;br /&gt;
&lt;br /&gt;
[[Other names]]:Butanoyl-CoA dehydrogenase, Butyryl dehydrogenase, Short-chain acyl CoA dehydrogenase, Unsatured acyl-CoA reductase.&lt;br /&gt;
&lt;br /&gt;
[[Enzyme class]]: E.C.1.3.8.1[https://enzyme.expasy.org/EC/1.3.8.1]&lt;br /&gt;
&lt;br /&gt;
[[Substrate]]: A short-chain acyl CoA &lt;br /&gt;
&lt;br /&gt;
[[Prosthetic group]]: 1 electron-transfer flavoprotein such as FDA, for every Subunits &lt;br /&gt;
&lt;br /&gt;
[[Products]]: a short-chain trans-2,3-dehydroacyl-CoA + reduced electron-transfer flavoprotein&lt;br /&gt;
&lt;br /&gt;
[[Pathways]]: Fatty acid degradation&lt;br /&gt;
&lt;br /&gt;
[[Other information]]:&lt;br /&gt;
&lt;br /&gt;
The enzyme from beef liver can accept acyl-chain lengths from 3 to 8 carbon atoms. From different organism the range can vary so we ignore if M.tuberculosis gets the same lengths resolution.&lt;br /&gt;
&lt;br /&gt;
The highest activity reported for beef liver enzyme was for substrates with 4 and 5 carbon acyl-chain lengths.&lt;br /&gt;
&lt;br /&gt;
==4IV6 as a research tool==&lt;br /&gt;
&lt;br /&gt;
4iv6 which belong to &#039;&#039;Mycobacterium tuberculosis&#039;&#039; was studied with other protein homolog.&lt;br /&gt;
They were chosen to be studied as potential TB-Drugs target&lt;br /&gt;
Studies have been made on homolog similarities aimed on their active site because with the knowledges of many homolog active site structure and how they work, we can design a inhibitor of those enzyme which can stop essential reaction and reduce or stop &#039;&#039;M.tuberculosis&#039;&#039; infection.&lt;br /&gt;
This strategy is called an « Homolog-rescue strategy ».&lt;br /&gt;
This strategy can be generalized for other drug target for other diseases.&lt;br /&gt;
&lt;br /&gt;
&lt;br /&gt;
== Structural highlights ==&lt;br /&gt;
&amp;lt;scene name=&#039;82/829361/Biological_unit/1&#039;&amp;gt;Biological unit&amp;lt;/scene&amp;gt;&lt;br /&gt;
&lt;br /&gt;
&amp;lt;scene name=&#039;82/829361/Asymetrical_unit/2&#039;&amp;gt;Asymetrical unit&amp;lt;/scene&amp;gt; :Light Grey:1st sub-unit, Light green:2nd sub-unit, Blue and red:FDA &lt;br /&gt;
&lt;br /&gt;
&amp;lt;scene name=&#039;82/829361/Secondary_structure/1&#039;&amp;gt;Secondary structure&amp;lt;/scene&amp;gt; : Red: helix alpha, Blue:FDA, Yellow: Beta sheet  &lt;br /&gt;
&lt;br /&gt;
&amp;lt;scene name=&#039;82/829361/Hydrophobic/1&#039;&amp;gt;Hydrophobic region&amp;lt;/scene&amp;gt; : Green: FDA, Purple: Polar region, Light grey: Hydrophobic region &lt;br /&gt;
&lt;br /&gt;
&amp;lt;/StructureSection&amp;gt;&lt;br /&gt;
== References ==&lt;br /&gt;
&amp;lt;references/&amp;gt;&lt;/div&gt;</summary>
		<author><name>Appoline Dubois</name></author>
	</entry>
	<entry>
		<id>https://proteopedia.org/index.php?title=Sandbox_Reserved_1108&amp;diff=3143115</id>
		<title>Sandbox Reserved 1108</title>
		<link rel="alternate" type="text/html" href="https://proteopedia.org/index.php?title=Sandbox_Reserved_1108&amp;diff=3143115"/>
		<updated>2020-01-14T17:39:40Z</updated>

		<summary type="html">&lt;p&gt;Appoline Dubois: &lt;/p&gt;
&lt;hr /&gt;
&lt;div&gt;{{Sandbox_ESBS_2019}}&amp;lt;!-- PLEASE ADD YOUR CONTENT BELOW HERE --&amp;gt;&lt;br /&gt;
==Your Heading Here (maybe something like &#039;Structure&#039;)==&lt;br /&gt;
&amp;lt;StructureSection load=&#039;1stp&#039; size=&#039;340&#039; side=&#039;right&#039; caption=&#039;Caption for this structure&#039; scene=&#039;&#039;&amp;gt;&lt;br /&gt;
This is a default text for your page &#039;&#039;&#039;&#039;&#039;&#039;. Click above on &#039;&#039;&#039;edit this page&#039;&#039;&#039; to modify. Be careful with the &amp;amp;lt; and &amp;amp;gt; signs.&lt;br /&gt;
You may include any references to papers as in: the use of JSmol in Proteopedia &amp;lt;ref&amp;gt;DOI 10.1002/ijch.201300024&amp;lt;/ref&amp;gt; or to the article describing Jmol &amp;lt;ref&amp;gt;PMID:21638687&amp;lt;/ref&amp;gt; to the rescue.&lt;br /&gt;
&lt;br /&gt;
== Function ==&lt;br /&gt;
==Primary and Secondary structure==&lt;br /&gt;
&lt;br /&gt;
Isovaleryl-CoA dehydrogenase is the assembly of &#039;&#039;&#039;&amp;lt;scene name=&#039;82/829361/2asymunit/1&#039;&amp;gt;two asymmetric units&amp;lt;/scene&amp;gt;&#039;&#039;&#039; each composed of &#039;&#039;&#039;two chains &amp;lt;scene name=&#039;82/829361/Chainea_asymunit/2&#039;&amp;gt;A&amp;lt;/scene&amp;gt; and &amp;lt;scene name=&#039;82/829361/Chaineb_asymunit/1&#039;&amp;gt;B&amp;lt;/scene&amp;gt;&#039;&#039;&#039; linked by a &amp;lt;scene name=&#039;82/829361/Ligand_asymunit/1&#039;&amp;gt;ligand&amp;lt;/scene&amp;gt; (Dihydroflavine-Adenine Dinucleotide). Each of the two chains A and B are composed of 388 amino acids. An asymmetric unit is therefore composed of 776 amino acids and has a molecular weight of 86233.70 Da.&lt;br /&gt;
&lt;br /&gt;
The A chain is made up of 17 helices (involving 221 residues) and 14 beta-sheets (61 residues).&lt;br /&gt;
Chain B is formed of 17 helices (involving 218 residues) and 14 beta-sheets (62 residues). &lt;br /&gt;
&lt;br /&gt;
==Tertiary structures==&lt;br /&gt;
==Enzymatic reaction==&lt;br /&gt;
&lt;br /&gt;
[[Enzyme accepted name]]: Short-chain acyl-CoA dehydrogenase&lt;br /&gt;
&lt;br /&gt;
[[Other names]]:Butanoyl-CoA dehydrogenase, Butyryl dehydrogenase, Short-chain acyl CoA dehydrogenase, Unsatured acyl-CoA reductase.&lt;br /&gt;
&lt;br /&gt;
[[Enzyme class]]: E.C.1.3.8.1[https://enzyme.expasy.org/EC/1.3.8.1]&lt;br /&gt;
&lt;br /&gt;
[[Substrate]]: A short-chain acyl CoA &lt;br /&gt;
&lt;br /&gt;
[[Prosthetic group]]: 1 electron-transfer flavoprotein such as FDA, for every Subunits &lt;br /&gt;
&lt;br /&gt;
[[Products]]: a short-chain trans-2,3-dehydroacyl-CoA + reduced electron-transfer flavoprotein&lt;br /&gt;
&lt;br /&gt;
[[Pathways]]: Fatty acid degradation&lt;br /&gt;
&lt;br /&gt;
[[Other information]]:&lt;br /&gt;
&lt;br /&gt;
The enzyme from beef liver can accept acyl-chain lengths from 3 to 8 carbon atoms. From different organism the range can vary so we ignore if M.tuberculosis gets the same lengths resolution.&lt;br /&gt;
&lt;br /&gt;
The highest activity reported for beef liver enzyme was for substrates with 4 and 5 carbon acyl-chain lengths.&lt;br /&gt;
&lt;br /&gt;
==4IV6 as a research tool==&lt;br /&gt;
&lt;br /&gt;
4iv6 which belong to &#039;&#039;Mycobacterium tuberculosis&#039;&#039; was studied with other protein homolog.&lt;br /&gt;
They were chosen to be studied as potential TB-Drugs target&lt;br /&gt;
Studies have been made on homolog similarities aimed on their active site because with the knowledges of many homolog active site structure and how they work, we can design a inhibitor of those enzyme which can stop essential reaction and reduce or stop &#039;&#039;M.tuberculosis&#039;&#039; infection.&lt;br /&gt;
This strategy is called an « Homolog-rescue strategy ».&lt;br /&gt;
This strategy can be generalized for other drug target for other diseases.&lt;br /&gt;
&lt;br /&gt;
&lt;br /&gt;
== Structural highlights ==&lt;br /&gt;
&amp;lt;scene name=&#039;82/829361/Biological_unit/1&#039;&amp;gt;Biological unit&amp;lt;/scene&amp;gt;&lt;br /&gt;
&lt;br /&gt;
&amp;lt;scene name=&#039;82/829361/Asymetrical_unit/2&#039;&amp;gt;Asymetrical unit&amp;lt;/scene&amp;gt; :Light Grey:1st sub-unit, Light green:2nd sub-unit, Blue and red:FDA &lt;br /&gt;
&lt;br /&gt;
&amp;lt;scene name=&#039;82/829361/Secondary_structure/1&#039;&amp;gt;Secondary structure&amp;lt;/scene&amp;gt; : Red: helix alpha, Blue:FDA, Yellow: Beta sheet  &lt;br /&gt;
&lt;br /&gt;
&amp;lt;scene name=&#039;82/829361/Hydrophobic/1&#039;&amp;gt;Hydrophobic region&amp;lt;/scene&amp;gt; : Green: FDA, Purple: Polar region, Light grey: Hydrophobic region &lt;br /&gt;
&lt;br /&gt;
&amp;lt;/StructureSection&amp;gt;&lt;br /&gt;
== References ==&lt;br /&gt;
&amp;lt;references/&amp;gt;&lt;/div&gt;</summary>
		<author><name>Appoline Dubois</name></author>
	</entry>
	<entry>
		<id>https://proteopedia.org/index.php?title=Sandbox_Reserved_1108&amp;diff=3143112</id>
		<title>Sandbox Reserved 1108</title>
		<link rel="alternate" type="text/html" href="https://proteopedia.org/index.php?title=Sandbox_Reserved_1108&amp;diff=3143112"/>
		<updated>2020-01-14T17:36:21Z</updated>

		<summary type="html">&lt;p&gt;Appoline Dubois: &lt;/p&gt;
&lt;hr /&gt;
&lt;div&gt;{{Sandbox_ESBS_2019}}&amp;lt;!-- PLEASE ADD YOUR CONTENT BELOW HERE --&amp;gt;&lt;br /&gt;
==Your Heading Here (maybe something like &#039;Structure&#039;)==&lt;br /&gt;
&amp;lt;StructureSection load=&#039;1stp&#039; size=&#039;340&#039; side=&#039;right&#039; caption=&#039;Caption for this structure&#039; scene=&#039;&#039;&amp;gt;&lt;br /&gt;
This is a default text for your page &#039;&#039;&#039;&#039;&#039;&#039;. Click above on &#039;&#039;&#039;edit this page&#039;&#039;&#039; to modify. Be careful with the &amp;amp;lt; and &amp;amp;gt; signs.&lt;br /&gt;
You may include any references to papers as in: the use of JSmol in Proteopedia &amp;lt;ref&amp;gt;DOI 10.1002/ijch.201300024&amp;lt;/ref&amp;gt; or to the article describing Jmol &amp;lt;ref&amp;gt;PMID:21638687&amp;lt;/ref&amp;gt; to the rescue.&lt;br /&gt;
&lt;br /&gt;
== Function ==&lt;br /&gt;
==Primary and Secondary structure==&lt;br /&gt;
&lt;br /&gt;
Isovaleryl-CoA dehydrogenase is the assembly of &#039;&#039;&#039;&amp;lt;scene name=&#039;82/829361/2asymunit/1&#039;&amp;gt;two asymmetric units&amp;lt;/scene&amp;gt;&#039;&#039;&#039; each composed of &#039;&#039;&#039;two chains &amp;lt;scene name=&#039;82/829361/Chainea_asymunit/2&#039;&amp;gt;A&amp;lt;/scene&amp;gt; and &amp;lt;scene name=&#039;82/829361/Chaineb_asymunit/1&#039;&amp;gt;B&amp;lt;/scene&amp;gt;&#039;&#039;&#039; linked by a ligand (Dihydroflavine-Adenine Dinucleotide). Each of the two chains A and B are composed of 388 amino acids. An asymmetric unit is therefore composed of 776 amino acids and has a molecular weight of 86233.70 Da.&lt;br /&gt;
&lt;br /&gt;
The A chain is made up of 17 helices (involving 221 residues) and 14 beta-sheets (61 residues).&lt;br /&gt;
Chain B is formed of 17 helices (involving 218 residues) and 14 beta-sheets (62 residues). &lt;br /&gt;
&lt;br /&gt;
==Tertiary structures==&lt;br /&gt;
==Enzymatic reaction==&lt;br /&gt;
&lt;br /&gt;
[[Enzyme accepted name]]: Short-chain acyl-CoA dehydrogenase&lt;br /&gt;
&lt;br /&gt;
[[Other names]]:Butanoyl-CoA dehydrogenase, Butyryl dehydrogenase, Short-chain acyl CoA dehydrogenase, Unsatured acyl-CoA reductase.&lt;br /&gt;
&lt;br /&gt;
[[Enzyme class]]: E.C.1.3.8.1[https://enzyme.expasy.org/EC/1.3.8.1]&lt;br /&gt;
&lt;br /&gt;
[[Substrate]]: A short-chain acyl CoA &lt;br /&gt;
&lt;br /&gt;
[[Prosthetic group]]: 1 electron-transfer flavoprotein such as FDA, for every Subunits &lt;br /&gt;
&lt;br /&gt;
[[Products]]: a short-chain trans-2,3-dehydroacyl-CoA + reduced electron-transfer flavoprotein&lt;br /&gt;
&lt;br /&gt;
[[Pathways]]: Fatty acid degradation&lt;br /&gt;
&lt;br /&gt;
[[Other information]]:&lt;br /&gt;
&lt;br /&gt;
The enzyme from beef liver can accept acyl-chain lengths from 3 to 8 carbon atoms. From different organism the range can vary so we ignore if M.tuberculosis gets the same lengths resolution.&lt;br /&gt;
&lt;br /&gt;
The highest activity reported for beef liver enzyme was for substrates with 4 and 5 carbon acyl-chain lengths.&lt;br /&gt;
&lt;br /&gt;
==4IV6 as a research tool==&lt;br /&gt;
&lt;br /&gt;
4iv6 which belong to &#039;&#039;Mycobacterium tuberculosis&#039;&#039; was studied with other protein homolog.&lt;br /&gt;
They were chosen to be studied as potential TB-Drugs target&lt;br /&gt;
Studies have been made on homolog similarities aimed on their active site because with the knowledges of many homolog active site structure and how they work, we can design a inhibitor of those enzyme which can stop essential reaction and reduce or stop &#039;&#039;M.tuberculosis&#039;&#039; infection.&lt;br /&gt;
This strategy is called an « Homolog-rescue strategy ».&lt;br /&gt;
This strategy can be generalized for other drug target for other diseases.&lt;br /&gt;
&lt;br /&gt;
&lt;br /&gt;
== Structural highlights ==&lt;br /&gt;
&amp;lt;scene name=&#039;82/829361/Biological_unit/1&#039;&amp;gt;Biological unit&amp;lt;/scene&amp;gt;&lt;br /&gt;
&lt;br /&gt;
&amp;lt;scene name=&#039;82/829361/Asymetrical_unit/2&#039;&amp;gt;Asymetrical unit&amp;lt;/scene&amp;gt; :Light Grey:1st sub-unit, Light green:2nd sub-unit, Blue and red:FDA &lt;br /&gt;
&lt;br /&gt;
&amp;lt;scene name=&#039;82/829361/Secondary_structure/1&#039;&amp;gt;Secondary structure&amp;lt;/scene&amp;gt; : Red: helix alpha, Blue:FDA, Yellow: Beta sheet  &lt;br /&gt;
&lt;br /&gt;
&amp;lt;scene name=&#039;82/829361/Hydrophobic/1&#039;&amp;gt;Hydrophobic region&amp;lt;/scene&amp;gt; : Green: FDA, Purple: Polar region, Light grey: Hydrophobic region &lt;br /&gt;
&lt;br /&gt;
&amp;lt;/StructureSection&amp;gt;&lt;br /&gt;
== References ==&lt;br /&gt;
&amp;lt;references/&amp;gt;&lt;/div&gt;</summary>
		<author><name>Appoline Dubois</name></author>
	</entry>
	<entry>
		<id>https://proteopedia.org/index.php?title=Sandbox_Reserved_1108&amp;diff=3143096</id>
		<title>Sandbox Reserved 1108</title>
		<link rel="alternate" type="text/html" href="https://proteopedia.org/index.php?title=Sandbox_Reserved_1108&amp;diff=3143096"/>
		<updated>2020-01-14T17:25:07Z</updated>

		<summary type="html">&lt;p&gt;Appoline Dubois: &lt;/p&gt;
&lt;hr /&gt;
&lt;div&gt;{{Sandbox_ESBS_2019}}&amp;lt;!-- PLEASE ADD YOUR CONTENT BELOW HERE --&amp;gt;&lt;br /&gt;
==Your Heading Here (maybe something like &#039;Structure&#039;)==&lt;br /&gt;
&amp;lt;StructureSection load=&#039;1stp&#039; size=&#039;340&#039; side=&#039;right&#039; caption=&#039;Caption for this structure&#039; scene=&#039;&#039;&amp;gt;&lt;br /&gt;
This is a default text for your page &#039;&#039;&#039;&#039;&#039;&#039;. Click above on &#039;&#039;&#039;edit this page&#039;&#039;&#039; to modify. Be careful with the &amp;amp;lt; and &amp;amp;gt; signs.&lt;br /&gt;
You may include any references to papers as in: the use of JSmol in Proteopedia &amp;lt;ref&amp;gt;DOI 10.1002/ijch.201300024&amp;lt;/ref&amp;gt; or to the article describing Jmol &amp;lt;ref&amp;gt;PMID:21638687&amp;lt;/ref&amp;gt; to the rescue.&lt;br /&gt;
&lt;br /&gt;
== Function ==&lt;br /&gt;
==Primary and Secondary structure==&lt;br /&gt;
&lt;br /&gt;
Isovaleryl-CoA dehydrogenase is the assembly of &#039;&#039;&#039;two asymmetric units&#039;&#039;&#039; each composed of &#039;&#039;&#039;two chains &amp;lt;scene name=&#039;82/829361/Chainea_asymunit/2&#039;&amp;gt;A&amp;lt;/scene&amp;gt; and B&#039;&#039;&#039; linked by a ligand (Dihydroflavine-Adenine Dinucleotide). Each of the two chains A and B are composed of 388 amino acids. An asymmetric unit is therefore composed of 776 amino acids and has a molecular weight of 86233.70 Da.&lt;br /&gt;
&lt;br /&gt;
The A chain is made up of 17 helices (involving 221 residues) and 14 beta-sheets (61 residues).&lt;br /&gt;
Chain B is formed of 17 helices (involving 218 residues) and 14 beta-sheets (62 residues). &lt;br /&gt;
&lt;br /&gt;
==Tertiary structures==&lt;br /&gt;
==Enzymatic reaction==&lt;br /&gt;
&lt;br /&gt;
[[Enzyme accepted name]]: Short-chain acyl-CoA dehydrogenase&lt;br /&gt;
&lt;br /&gt;
[[Other names]]:Butanoyl-CoA dehydrogenase, Butyryl dehydrogenase, Short-chain acyl CoA dehydrogenase, Unsatured acyl-CoA reductase.&lt;br /&gt;
&lt;br /&gt;
[[Enzyme class]]: E.C.1.3.8.1[https://enzyme.expasy.org/EC/1.3.8.1]&lt;br /&gt;
&lt;br /&gt;
[[Substrate]]: A short-chain acyl CoA &lt;br /&gt;
&lt;br /&gt;
[[Prosthetic group]]: 1 electron-transfer flavoprotein such as FDA, for every Subunits &lt;br /&gt;
&lt;br /&gt;
[[Products]]: a short-chain trans-2,3-dehydroacyl-CoA + reduced electron-transfer flavoprotein&lt;br /&gt;
&lt;br /&gt;
[[Pathways]]: Fatty acid degradation&lt;br /&gt;
&lt;br /&gt;
[[Other information]]:&lt;br /&gt;
&lt;br /&gt;
The enzyme from beef liver can accept acyl-chain lengths from 3 to 8 carbon atoms. From different organism the range can vary so we ignore if M.tuberculosis gets the same lengths resolution.&lt;br /&gt;
&lt;br /&gt;
The highest activity reported for beef liver enzyme was for substrates with 4 and 5 carbon acyl-chain lengths.&lt;br /&gt;
&lt;br /&gt;
==4IV6 as a research tool==&lt;br /&gt;
&lt;br /&gt;
4iv6 which belong to &#039;&#039;Mycobacterium tuberculosis&#039;&#039; was studied with other protein homolog.&lt;br /&gt;
They were chosen to be studied as potential TB-Drugs target&lt;br /&gt;
Studies have been made on homolog similarities aimed on their active site because with the knowledges of many homolog active site structure and how they work, we can design a inhibitor of those enzyme which can stop essential reaction and reduce or stop &#039;&#039;M.tuberculosis&#039;&#039; infection.&lt;br /&gt;
This strategy is called an « Homolog-rescue strategy ».&lt;br /&gt;
This strategy can be generalized for other drug target for other diseases.&lt;br /&gt;
&lt;br /&gt;
&lt;br /&gt;
== Structural highlights ==&lt;br /&gt;
&amp;lt;scene name=&#039;82/829361/Biological_unit/1&#039;&amp;gt;Biological unit&amp;lt;/scene&amp;gt;&lt;br /&gt;
&lt;br /&gt;
&amp;lt;scene name=&#039;82/829361/Asymetrical_unit/2&#039;&amp;gt;Asymetrical unit&amp;lt;/scene&amp;gt; :Light Grey:1st sub-unit, Light green:2nd sub-unit, Blue and red:FDA &lt;br /&gt;
&lt;br /&gt;
&amp;lt;scene name=&#039;82/829361/Secondary_structure/1&#039;&amp;gt;Secondary structure&amp;lt;/scene&amp;gt; : Red: helix alpha, Blue:FDA, Yellow: Beta sheet  &lt;br /&gt;
&lt;br /&gt;
&amp;lt;scene name=&#039;82/829361/Hydrophobic/1&#039;&amp;gt;Hydrophobic region&amp;lt;/scene&amp;gt; : Green: FDA, Purple: Polar region, Light grey: Hydrophobic region &lt;br /&gt;
&lt;br /&gt;
&amp;lt;/StructureSection&amp;gt;&lt;br /&gt;
== References ==&lt;br /&gt;
&amp;lt;references/&amp;gt;&lt;/div&gt;</summary>
		<author><name>Appoline Dubois</name></author>
	</entry>
	<entry>
		<id>https://proteopedia.org/index.php?title=Sandbox_Reserved_1108&amp;diff=3143093</id>
		<title>Sandbox Reserved 1108</title>
		<link rel="alternate" type="text/html" href="https://proteopedia.org/index.php?title=Sandbox_Reserved_1108&amp;diff=3143093"/>
		<updated>2020-01-14T17:21:58Z</updated>

		<summary type="html">&lt;p&gt;Appoline Dubois: &lt;/p&gt;
&lt;hr /&gt;
&lt;div&gt;{{Sandbox_ESBS_2019}}&amp;lt;!-- PLEASE ADD YOUR CONTENT BELOW HERE --&amp;gt;&lt;br /&gt;
==Your Heading Here (maybe something like &#039;Structure&#039;)==&lt;br /&gt;
&amp;lt;StructureSection load=&#039;1stp&#039; size=&#039;340&#039; side=&#039;right&#039; caption=&#039;Caption for this structure&#039; scene=&#039;&#039;&amp;gt;&lt;br /&gt;
This is a default text for your page &#039;&#039;&#039;&#039;&#039;&#039;. Click above on &#039;&#039;&#039;edit this page&#039;&#039;&#039; to modify. Be careful with the &amp;amp;lt; and &amp;amp;gt; signs.&lt;br /&gt;
You may include any references to papers as in: the use of JSmol in Proteopedia &amp;lt;ref&amp;gt;DOI 10.1002/ijch.201300024&amp;lt;/ref&amp;gt; or to the article describing Jmol &amp;lt;ref&amp;gt;PMID:21638687&amp;lt;/ref&amp;gt; to the rescue.&lt;br /&gt;
&lt;br /&gt;
== Function ==&lt;br /&gt;
==Primary and Secondary structure==&lt;br /&gt;
&lt;br /&gt;
Isovaleryl-CoA dehydrogenase is the assembly of &#039;&#039;&#039;two asymmetric units&#039;&#039;&#039; each composed of &#039;&#039;&#039;two chains &amp;lt;scene name=&#039;82/829361/Chainea_asymunit/1&#039;&amp;gt;A&amp;lt;/scene&amp;gt; and B&#039;&#039;&#039; linked by a ligand (Dihydroflavine-Adenine Dinucleotide). Each of the two chains A and B are composed of 388 amino acids. An asymmetric unit is therefore composed of 776 amino acids and has a molecular weight of 86233.70 Da.&lt;br /&gt;
&lt;br /&gt;
The A chain is made up of 17 helices (involving 221 residues) and 14 beta-sheets (61 residues).&lt;br /&gt;
Chain B is formed of 17 helices (involving 218 residues) and 14 beta-sheets (62 residues). &lt;br /&gt;
&lt;br /&gt;
==Tertiary structures==&lt;br /&gt;
==Enzymatic reaction==&lt;br /&gt;
&lt;br /&gt;
[[Enzyme accepted name]]: Short-chain acyl-CoA dehydrogenase&lt;br /&gt;
&lt;br /&gt;
[[Other names]]:Butanoyl-CoA dehydrogenase, Butyryl dehydrogenase, Short-chain acyl CoA dehydrogenase, Unsatured acyl-CoA reductase.&lt;br /&gt;
&lt;br /&gt;
[[Enzyme class]]: E.C.1.3.8.1[https://enzyme.expasy.org/EC/1.3.8.1]&lt;br /&gt;
&lt;br /&gt;
[[Substrate]]: A short-chain acyl CoA &lt;br /&gt;
&lt;br /&gt;
[[Prosthetic group]]: 1 electron-transfer flavoprotein such as FDA, for every Subunits &lt;br /&gt;
&lt;br /&gt;
[[Products]]: a short-chain trans-2,3-dehydroacyl-CoA + reduced electron-transfer flavoprotein&lt;br /&gt;
&lt;br /&gt;
[[Pathways]]: Fatty acid degradation&lt;br /&gt;
&lt;br /&gt;
[[Other information]]:&lt;br /&gt;
&lt;br /&gt;
The enzyme from beef liver can accept acyl-chain lengths from 3 to 8 carbon atoms. From different organism the range can vary so we ignore if M.tuberculosis gets the same lengths resolution.&lt;br /&gt;
&lt;br /&gt;
The highest activity reported for beef liver enzyme was for substrates with 4 and 5 carbon acyl-chain lengths.&lt;br /&gt;
&lt;br /&gt;
==4IV6 as a research tool==&lt;br /&gt;
&lt;br /&gt;
4iv6 which belong to &#039;&#039;Mycobacterium tuberculosis&#039;&#039; was studied with other protein homolog.&lt;br /&gt;
They were chosen to be studied as potential TB-Drugs target&lt;br /&gt;
Studies have been made on homolog similarities aimed on their active site because with the knowledges of many homolog active site structure and how they work, we can design a inhibitor of those enzyme which can stop essential reaction and reduce or stop &#039;&#039;M.tuberculosis&#039;&#039; infection.&lt;br /&gt;
This strategy is called an « Homolog-rescue strategy ».&lt;br /&gt;
This strategy can be generalized for other drug target for other diseases.&lt;br /&gt;
&lt;br /&gt;
&lt;br /&gt;
== Structural highlights ==&lt;br /&gt;
&amp;lt;scene name=&#039;82/829361/Biological_unit/1&#039;&amp;gt;Biological unit&amp;lt;/scene&amp;gt;&lt;br /&gt;
&lt;br /&gt;
&amp;lt;scene name=&#039;82/829361/Asymetrical_unit/2&#039;&amp;gt;Asymetrical unit&amp;lt;/scene&amp;gt; :Light Grey:1st sub-unit, Light green:2nd sub-unit, Blue and red:FDA &lt;br /&gt;
&lt;br /&gt;
&amp;lt;scene name=&#039;82/829361/Secondary_structure/1&#039;&amp;gt;Secondary structure&amp;lt;/scene&amp;gt; : Red: helix alpha, Blue:FDA, Yellow: Beta sheet  &lt;br /&gt;
&lt;br /&gt;
&amp;lt;scene name=&#039;82/829361/Hydrophobic/1&#039;&amp;gt;Hydrophobic region&amp;lt;/scene&amp;gt; : Green: FDA, Purple: Polar region, Light grey: Hydrophobic region &lt;br /&gt;
&lt;br /&gt;
&amp;lt;/StructureSection&amp;gt;&lt;br /&gt;
== References ==&lt;br /&gt;
&amp;lt;references/&amp;gt;&lt;/div&gt;</summary>
		<author><name>Appoline Dubois</name></author>
	</entry>
	<entry>
		<id>https://proteopedia.org/index.php?title=Sandbox_Reserved_1108&amp;diff=3143069</id>
		<title>Sandbox Reserved 1108</title>
		<link rel="alternate" type="text/html" href="https://proteopedia.org/index.php?title=Sandbox_Reserved_1108&amp;diff=3143069"/>
		<updated>2020-01-14T16:51:49Z</updated>

		<summary type="html">&lt;p&gt;Appoline Dubois: &lt;/p&gt;
&lt;hr /&gt;
&lt;div&gt;{{Sandbox_ESBS_2019}}&amp;lt;!-- PLEASE ADD YOUR CONTENT BELOW HERE --&amp;gt;&lt;br /&gt;
==Your Heading Here (maybe something like &#039;Structure&#039;)==&lt;br /&gt;
&amp;lt;StructureSection load=&#039;1stp&#039; size=&#039;340&#039; side=&#039;right&#039; caption=&#039;Caption for this structure&#039; scene=&#039;&#039;&amp;gt;&lt;br /&gt;
This is a default text for your page &#039;&#039;&#039;&#039;&#039;&#039;. Click above on &#039;&#039;&#039;edit this page&#039;&#039;&#039; to modify. Be careful with the &amp;amp;lt; and &amp;amp;gt; signs.&lt;br /&gt;
You may include any references to papers as in: the use of JSmol in Proteopedia &amp;lt;ref&amp;gt;DOI 10.1002/ijch.201300024&amp;lt;/ref&amp;gt; or to the article describing Jmol &amp;lt;ref&amp;gt;PMID:21638687&amp;lt;/ref&amp;gt; to the rescue.&lt;br /&gt;
&lt;br /&gt;
== Function ==&lt;br /&gt;
==Primary and Secondary structure==&lt;br /&gt;
&lt;br /&gt;
Isovaleryl-CoA dehydrogenase is the assembly of &#039;&#039;&#039;two asymmetric units&#039;&#039;&#039; each composed of &#039;&#039;&#039;two chains A and B&#039;&#039;&#039; linked by a ligand (Dihydroflavine-Adenine Dinucleotide). Each of the two chains A and B are composed of 388 amino acids. An asymmetric unit is therefore composed of 776 amino acids and has a molecular weight of 86233.70 Da.&lt;br /&gt;
&lt;br /&gt;
The A chain is made up of 17 helices (involving 221 residues) and 14 beta-sheets (61 residues).&lt;br /&gt;
Chain B is formed of 17 helices (involving 218 residues) and 14 beta-sheets (62 residues). &lt;br /&gt;
&lt;br /&gt;
==Tertiary structures==&lt;br /&gt;
==Enzymatic reaction==&lt;br /&gt;
&lt;br /&gt;
[[Enzyme accepted name]]: Short-chain acyl-CoA dehydrogenase&lt;br /&gt;
&lt;br /&gt;
[[Other names]]:Butanoyl-CoA dehydrogenase, Butyryl dehydrogenase, Short-chain acyl CoA dehydrogenase, Unsatured acyl-CoA reductase.&lt;br /&gt;
&lt;br /&gt;
[[Enzyme class]]: E.C.1.3.8.1[https://enzyme.expasy.org/EC/1.3.8.1]&lt;br /&gt;
&lt;br /&gt;
[[Substrate]]: A short-chain acyl CoA &lt;br /&gt;
&lt;br /&gt;
[[Prosthetic group]]: 1 electron-transfer flavoprotein such as FDA, for every Subunits &lt;br /&gt;
&lt;br /&gt;
[[Products]]: a short-chain trans-2,3-dehydroacyl-CoA + reduced electron-transfer flavoprotein&lt;br /&gt;
&lt;br /&gt;
[[Pathways]]: Fatty acid degradation&lt;br /&gt;
&lt;br /&gt;
[[Other information]]:&lt;br /&gt;
&lt;br /&gt;
The enzyme from beef liver can accept acyl-chain lengths from 3 to 8 carbon atoms. From different organism the range can vary so we ignore if M.tuberculosis gets the same lengths resolution.&lt;br /&gt;
&lt;br /&gt;
The highest activity reported for beef liver enzyme was for substrates with 4 and 5 carbon acyl-chain lengths.&lt;br /&gt;
&lt;br /&gt;
==4IV6 as a research tool==&lt;br /&gt;
&lt;br /&gt;
4iv6 which belong to &#039;&#039;Mycobacterium tuberculosis&#039;&#039; was studied with other protein homolog.&lt;br /&gt;
They were chosen to be studied as potential TB-Drugs target&lt;br /&gt;
Studies have been made on homolog similarities aimed on their active site because with the knowledges of many homolog active site structure and how they work, we can design a inhibitor of those enzyme which can stop essential reaction and reduce or stop &#039;&#039;M.tuberculosis&#039;&#039; infection.&lt;br /&gt;
This strategy is called an « Homolog-rescue strategy ».&lt;br /&gt;
This strategy can be generalized for other drug target for other diseases.&lt;br /&gt;
&lt;br /&gt;
&lt;br /&gt;
== Structural highlights ==&lt;br /&gt;
&amp;lt;scene name=&#039;82/829361/Biological_unit/1&#039;&amp;gt;Biological unit&amp;lt;/scene&amp;gt;&lt;br /&gt;
&lt;br /&gt;
&amp;lt;scene name=&#039;82/829361/Asymetrical_unit/2&#039;&amp;gt;Asymetrical unit&amp;lt;/scene&amp;gt; :Light Grey:1st sub-unit, Light green:2nd sub-unit, Blue and red:FDA &lt;br /&gt;
&lt;br /&gt;
&amp;lt;scene name=&#039;82/829361/Secondary_structure/1&#039;&amp;gt;Secondary structure&amp;lt;/scene&amp;gt; : Red: helix alpha, Blue:FDA, Yellow: Beta sheet  &lt;br /&gt;
&lt;br /&gt;
&amp;lt;scene name=&#039;82/829361/Hydrophobic/1&#039;&amp;gt;Hydrophobic region&amp;lt;/scene&amp;gt; : Green: FDA, Purple: Polar region, Light grey: Hydrophobic region &lt;br /&gt;
&lt;br /&gt;
&amp;lt;/StructureSection&amp;gt;&lt;br /&gt;
== References ==&lt;br /&gt;
&amp;lt;references/&amp;gt;&lt;/div&gt;</summary>
		<author><name>Appoline Dubois</name></author>
	</entry>
	<entry>
		<id>https://proteopedia.org/index.php?title=Sandbox_Reserved_1108&amp;diff=3143059</id>
		<title>Sandbox Reserved 1108</title>
		<link rel="alternate" type="text/html" href="https://proteopedia.org/index.php?title=Sandbox_Reserved_1108&amp;diff=3143059"/>
		<updated>2020-01-14T16:23:44Z</updated>

		<summary type="html">&lt;p&gt;Appoline Dubois: &lt;/p&gt;
&lt;hr /&gt;
&lt;div&gt;{{Sandbox_ESBS_2019}}&amp;lt;!-- PLEASE ADD YOUR CONTENT BELOW HERE --&amp;gt;&lt;br /&gt;
==Your Heading Here (maybe something like &#039;Structure&#039;)==&lt;br /&gt;
&amp;lt;StructureSection load=&#039;1stp&#039; size=&#039;340&#039; side=&#039;right&#039; caption=&#039;Caption for this structure&#039; scene=&#039;&#039;&amp;gt;&lt;br /&gt;
This is a default text for your page &#039;&#039;&#039;&#039;&#039;&#039;. Click above on &#039;&#039;&#039;edit this page&#039;&#039;&#039; to modify. Be careful with the &amp;amp;lt; and &amp;amp;gt; signs.&lt;br /&gt;
You may include any references to papers as in: the use of JSmol in Proteopedia &amp;lt;ref&amp;gt;DOI 10.1002/ijch.201300024&amp;lt;/ref&amp;gt; or to the article describing Jmol &amp;lt;ref&amp;gt;PMID:21638687&amp;lt;/ref&amp;gt; to the rescue.&lt;br /&gt;
&lt;br /&gt;
== Function ==&lt;br /&gt;
==Primary and Secondary structure==&lt;br /&gt;
&lt;br /&gt;
Isovaleryl-CoA dehydrogenase is the assembly of two asymmetric units each composed of two chains A and B linked by a ligand (Dihydroflavine-Adenine Dinucleotide). Each of the two chains A and B are composed of 388 amino acids. An asymmetric unit is therefore composed of 776 amino acids and has a molecular weight of 86233.70 Da.&lt;br /&gt;
&lt;br /&gt;
The A chain is made up of 17 helices (involving 221 residues) and 14 beta-sheets (61 residues).&lt;br /&gt;
Chain B is formed of 17 helices (involving 218 residues) and 14 beta-sheets (62 residues). &lt;br /&gt;
&lt;br /&gt;
==Tertiary structures==&lt;br /&gt;
==Enzymatic reaction==&lt;br /&gt;
&lt;br /&gt;
[[Enzyme accepted name]]: Short-chain acyl-CoA dehydrogenase&lt;br /&gt;
&lt;br /&gt;
[[Other names]]:Butanoyl-CoA dehydrogenase, Butyryl dehydrogenase, Short-chain acyl CoA dehydrogenase, Unsatured acyl-CoA reductase.&lt;br /&gt;
&lt;br /&gt;
[[Enzyme class]]: E.C.1.3.8.1[https://enzyme.expasy.org/EC/1.3.8.1]&lt;br /&gt;
&lt;br /&gt;
[[Substrate]]: A short-chain acyl CoA &lt;br /&gt;
&lt;br /&gt;
[[Prosthetic group]]: 1 electron-transfer flavoprotein such as FDA, for every Subunits &lt;br /&gt;
&lt;br /&gt;
[[Products]]: a short-chain trans-2,3-dehydroacyl-CoA + reduced electron-transfer flavoprotein&lt;br /&gt;
&lt;br /&gt;
[[Pathways]]: Fatty acid degradation&lt;br /&gt;
&lt;br /&gt;
[[Other information]]:&lt;br /&gt;
&lt;br /&gt;
The enzyme from beef liver can accept acyl-chain lengths from 3 to 8 carbon atoms. From different organism the range can vary so we ignore if M.tuberculosis gets the same lengths resolution.&lt;br /&gt;
&lt;br /&gt;
The highest activity reported for beef liver enzyme was for substrates with 4 and 5 carbon acyl-chain lengths.&lt;br /&gt;
&lt;br /&gt;
==4IV6 as a research tool==&lt;br /&gt;
&lt;br /&gt;
4iv6 which belong to &#039;&#039;Mycobacterium tuberculosis&#039;&#039; was studied with other protein homolog.&lt;br /&gt;
They were chosen to be studied as potential TB-Drugs target&lt;br /&gt;
Studies have been made on homolog similarities aimed on their active site because with the knowledges of many homolog active site structure and how they work, we can design a inhibitor of those enzyme which can stop essential reaction and reduce or stop &#039;&#039;M.tuberculosis&#039;&#039; infection.&lt;br /&gt;
This strategy is called an « Homolog-rescue strategy ».&lt;br /&gt;
This strategy can be generalized for other drug target for other diseases.&lt;br /&gt;
&lt;br /&gt;
&lt;br /&gt;
== Structural highlights ==&lt;br /&gt;
&amp;lt;scene name=&#039;82/829361/Biological_unit/1&#039;&amp;gt;Biological unit&amp;lt;/scene&amp;gt;&lt;br /&gt;
&lt;br /&gt;
&amp;lt;scene name=&#039;82/829361/Asymetrical_unit/2&#039;&amp;gt;Asymetrical unit&amp;lt;/scene&amp;gt; :Light Grey:1st sub-unit, Light green:2nd sub-unit, Blue and red:FDA &lt;br /&gt;
&lt;br /&gt;
&amp;lt;scene name=&#039;82/829361/Secondary_structure/1&#039;&amp;gt;Secondary structure&amp;lt;/scene&amp;gt; : Red: helix alpha, Blue:FDA, Yellow: Beta sheet  &lt;br /&gt;
&lt;br /&gt;
&amp;lt;scene name=&#039;82/829361/Hydrophobic/1&#039;&amp;gt;Hydrophobic region&amp;lt;/scene&amp;gt; : Green: FDA, Purple: Polar region, Light grey: Hydrophobic region &lt;br /&gt;
&lt;br /&gt;
&amp;lt;/StructureSection&amp;gt;&lt;br /&gt;
== References ==&lt;br /&gt;
&amp;lt;references/&amp;gt;&lt;/div&gt;</summary>
		<author><name>Appoline Dubois</name></author>
	</entry>
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