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Sandbox Reserved 1108

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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).
Chain B is formed of <scene name='82/829361/Helixchainb_asymunit/1'>17 helices</scene> (involving 218 residues) and <scene name='82/829361/Betasheetchainb_asymunit/1'>14 beta-sheets</scene> (62 residues).
Chain B is formed of <scene name='82/829361/Helixchainb_asymunit/1'>17 helices</scene> (involving 218 residues) and <scene name='82/829361/Betasheetchainb_asymunit/1'>14 beta-sheets</scene> (62 residues).
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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>
==Tertiary structures==
==Tertiary structures==
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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. <ref>https://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4iv6</ref>
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The assymetric unit contains 2 ligands: 2FDA, Dihydroflavine-adenine dinucleotide.
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The assymetric unit also contains 2 ligands: 2FDA, Dihydroflavine-adenine dinucleotide.
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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>
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>

Revision as of 16:21, 17 January 2020

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

Caption for this structure

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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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