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. 2016 Jul 26;7:1160. doi: 10.3389/fmicb.2016.01160

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Copyright © 2016 Arenas-Salinas, Vargas-Pérez, Morales, Pinto, Muñoz-Díaz, Cornejo, Pugin, Sandoval, Díaz-Vásquez, Muñoz-Villagrán, Rodríguez-Rojas, Morales, Vásquez and Arenas.

This is an open-access article distributed under the terms of the Creative Commons Attribution License (CC BY). The use, distribution or reproduction in other forums is permitted, provided the original author(s) or licensor are credited and that the original publication in this journal is cited, in accordance with accepted academic practice. No use, distribution or reproduction is permitted which does not comply with these terms.

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In silico analysis of E. coli TR flavoproteins. E3 (PDB_ID: 4JDR, green), GorA (PDB_ID: 1GER, cyan), AhpF (PDB_ID: 1FL2, purple), and TrxB (PDB_ID: 1CL0, yellow) flavoproteins are shown. (A) Structure alignment of these proteins showing their 3D structure available in PDB data base (Raptor X software; Wang S. et al., 2011). The global RMSD was 3.61 Å. (B) Structure alignment for the FAD molecule and representation of the interaction with the two catalytic cysteine residues of each protein. (C) Representation of the pyridine nucleotide-disulphide oxidoreductases class-I and class-II active sites.