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A, the Fo - Fc simulated annealing omit map for the FAD cofactor contoured at the 2 σ level. This density map clearly displays that the C130A mutant still retains the 8α-N1-histidyl bond but not the 6-S-cysteinyl bond. B, superposition of the active-site residues in the wild-type (black) and C130A (cyan) structures. The noncovalent contacts between the flavin C-6 and the Ala130 Cβ atoms result in Thr129 and Tyr300 shifting away from the substrate-binding site.
