Sandbox Reserved 1108
From Proteopedia
(Difference between revisions)
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==Tertiary structures== | ==Tertiary structures== | ||
- | 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. | + | 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> |
The assymetric unit also contains 2 ligands: 2FDA, Dihydroflavine-adenine dinucleotide. | The assymetric unit also contains 2 ligands: 2FDA, Dihydroflavine-adenine dinucleotide. | ||
- | 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. | + | 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>== |
Revision as of 15:41, 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
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References
- ↑ http://www.rcsb.org/structure/4IV6
- ↑ https://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4iv6
- ↑ https://en.wikipedia.org/wiki/Flavin_adenine_dinucleotide
- ↑ http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl?pdbcode=4iv6
- ↑ https://www.ebi.ac.uk/intenz/query?cmd=SearchEC&ec=1.3.8.1
- ↑ https://enzyme.expasy.org/EC/1.3.8.1