Fig. 1: Falcilysin domain and sequence structure. | Communications Biology

Fig. 1: Falcilysin domain and sequence structure.

From: Inhibition of falcilysin from Plasmodium falciparum by interference with its closed-to-open dynamic transition

Fig. 1

A Schematic representation of FLN domain structure with catalytic residues labeled. Helix α13, proposed to act as a hinge region in the open-to-closed transition, is labeled. B Amino-acid sequence of FLN with the secondary structure displayed on top of the sequence. The catalytic residue E132, as well as zinc-coordinating residues H129, H133, and E243, are colored in red. Residues from helix α13 are in bold. Linker residues connecting N-half and C-half are underlined. The figure was generated using ESPript. η: 310-helix, TT: β-turn and TTT: α turn.

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