Sandbox Reserved 1108

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4iv6 functions were not studied and only structural infos are disponible.
4iv6 functions were not studied and only structural infos are disponible.
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.
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.
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Butyryl-CoA Dehydrogenase[https://meshb.nlm.nih.gov/record/ui?name=Short-chain%20acyl-CoA%20dehydrogenase].
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E.C.1.3.8.1[https://enzyme.expasy.org/EC/1.3.8.1] is communly found in following pathways with various functions:
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[[Analine metabolism]]:[https://www.brenda-enzymes.info/pathway_index.php?pathway=alanine%20metabolism&ecno=1.3.8.1]
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[[Butanoate metabolism]]:[https://www.genome.jp/kegg-bin/show_pathway?map00650+1.3.8.1]
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[[Lipids metabolism]] : [https://www.brenda-enzymes.info/pathway_index.php?pathway=lipid%20metabolism&ecno=1.3.8.1][https://www.genome.jp/kegg-bin/show_pathway?map00071+1.3.8.1]
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[[Valine Leucine and isoleucine pathways]]:[https://www.genome.jp/kegg-bin/show_pathway?map00280+1.3.8.1]
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==Primary and Secondary structure<ref>http://www.rcsb.org/structure/4IV6</ref>==
==Primary and Secondary structure<ref>http://www.rcsb.org/structure/4IV6</ref>==
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Isovaleryl-CoA dehydrogenase is the assembly of '''<scene name='82/829361/2asymunit/1'>two asymmetric units</scene>''' each composed of '''two chains <scene name='82/829361/Chainea_asymunit/2'>A</scene> and <scene name='82/829361/Chaineb_asymunit/1'>B</scene>''' linked by a <scene name='82/829361/Ligand_asymunit/1'>ligand</scene> (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.
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Isovaleryl-CoA dehydrogenase is the assembly of '''<scene name='82/829361/2asymunit/1'>two asymmetric units</scene>''' each composed of '''two chains <scene name='82/829361/Chainea_asymunit/2'>A</scene> and <scene name='82/829361/Chaineb_asymunit/1'>B</scene>'''. 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.
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1% of the unit's amino acid have incomplete sidechains, which means that there are 11 missing residue in the assymetric unit.<ref>https://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4iv6</ref>
The A chain is made up of <scene name='82/829361/Helixalphachaina_asymunit/1'>17 helices</scene> (involving 221 residues) and <scene name='82/829361/Betasheetchaina_asymunit/1'>14 beta-sheets</scene> (61 residues).
The A chain is made up of <scene name='82/829361/Helixalphachaina_asymunit/1'>17 helices</scene> (involving 221 residues) and <scene name='82/829361/Betasheetchaina_asymunit/1'>14 beta-sheets</scene> (61 residues).
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==Tertiary structures==
==Tertiary structures==
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The two chains A and B of the isovaleryl-CoA dehydrogenase are linked by a <scene name='82/829361/Ligand_asymunit/1'>ligand</scene> (Dihydroflavine-Adenine Dinucleotide also known as [https://pubchem.ncbi.nlm.nih.gov/compound/Dihydroflavine-adenine-dinucleotide FADH2] ).
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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. <ref>https://en.wikipedia.org/wiki/Flavin_adenine_dinucleotide</ref>
==Enzymatic reaction<ref>http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl?pdbcode=4iv6</ref><ref>https://www.ebi.ac.uk/intenz/query?cmd=SearchEC&ec=1.3.8.1</ref><ref>https://enzyme.expasy.org/EC/1.3.8.1</ref>==
==Enzymatic reaction<ref>http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl?pdbcode=4iv6</ref><ref>https://www.ebi.ac.uk/intenz/query?cmd=SearchEC&ec=1.3.8.1</ref><ref>https://enzyme.expasy.org/EC/1.3.8.1</ref>==

Current revision

This Sandbox is Reserved from 25/11/2019, through 30/9/2020 for use in the course "Structural Biology" taught by Bruno Kieffer at the University of Strasbourg, ESBS. This reservation includes Sandbox Reserved 1091 through Sandbox Reserved 1115.
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4iv6

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References

  1. ↑ http://www.rcsb.org/structure/4IV6
  2. ↑ https://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4iv6
  3. ↑ https://en.wikipedia.org/wiki/Flavin_adenine_dinucleotide
  4. ↑ http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl?pdbcode=4iv6
  5. ↑ https://www.ebi.ac.uk/intenz/query?cmd=SearchEC&ec=1.3.8.1
  6. ↑ https://enzyme.expasy.org/EC/1.3.8.1
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