Extended Data Fig. 6: ACP1a interaction with KS, KS-AT linker domain, and AT-ACP2 linker. | Nature Structural & Molecular Biology

Extended Data Fig. 6: ACP1a interaction with KS, KS-AT linker domain, and AT-ACP2 linker.

From: Structure and dynamics of the essential endogenous mycobacterial polyketide synthase Pks13

Extended Data Fig. 6: ACP1a interaction with KS, KS-AT linker domain, and AT-ACP2 linker.

Interfacing residues between ACP1a and KS, KS-AT linker domain, and AT-ACP2 linker are shown as stick representation and labeled. Pi-pi stacking interaction is shown between R63 of ACP1a and R496 of KS. The Ppant arm is shown attached to S38 in helix II of ACP1a, and Ppant density is shown zoned around 2.3 Å around the model.

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