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. 2020 Jan 27;64(2):e01899-19. doi: 10.1128/AAC.01899-19

FIG 1.

FIG 1

Structural organization of KatGMtb. (a) Schematic representation of KatGMtb domains and important residues in the heme distal pocket (red), heme proximal pocket (purple), covalent triad (blue), dimerization domain (orange), and suggested INH gating channel for heme access channel (pink). (b and c) Structural arrangement of the residues in the heme active site (c) and the structure of a KatG monomer, based on KatGMtb (PDB ID 1SJ2).