Extended Data Fig. 6: Close-up views of key residues in FeSII that were previously investigated for mutational effects in literature. | Nature

Extended Data Fig. 6: Close-up views of key residues in FeSII that were previously investigated for mutational effects in literature.

From: Structural basis for the conformational protection of nitrogenase from O2

Extended Data Fig. 6

a, ε¹H56 and ε2K16 (in grey) exhibit intramolecular hydrogen bonding between ε¹E109 and ε¹D110, respectively. b, Interaction of ε¹H13 with MoFeP’ α1’E288 accompanied by ε¹H56, ε¹K15, ε¹K16, ε2K16 (in grey) shown in the background. c, ε¹K15 and ε¹K16 (in grey) and the interaction of the latter with ε2D110. d, ε¹K70 and ε¹K71 (in grey) and the interaction of the former with the backbone carbonyl of ε¹D44 and the latter with ε¹R99.

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