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. 2016 Nov 28;6:37610. doi: 10.1038/srep37610

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Copyright © 2016, The Author(s)

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(A) Crystal structure of oxidized EcAhpC_1-186-YFSKHN in decameric form (α₂)₅. Each subunit in the basic functional dimeric unit is shown in light and bright colors denoted as A and A’. The intermolecular disulphide bond between the peroxidatic (C_P) and resolving (C_R’) cysteine is shown in ball representation. (B) The 2F_O-F_C map contour at 1 σ level around the C_P and C_R’ in disulphide bond conformation. (C) Each subunit is composed of two interface regions, namely the dimer and oligomer interface. The secondary structural features are highlighted according to their position in the structure. (D) The average main chain B-factor of ten chains showed three highly dynamic regions in the structure.