Extended Data Fig. 1: Overall structure of EasCCf and comparison to Human Erythrocyte Catalase (HEC).
From: Chanoclavine synthase operates by an NADPH-independent superoxide mechanism
a, EasCCf’s oligomerization status. b, Cartoon model of EasCCf monomer. No NADPH can be found in the NADPH binding pocket. c, The SEC analysis of EasCCf. The blue and red traces represent EasCCf and a marker that contains six proteins with known molecular mass. The theoretical and calculated molecular mass of EasCCf is 53.98 and 102.45 kDa, respectively, suggesting that EasCCf should exist as a dimer in solution. d, HEC’s oligomerization status. e, Cartoon model of HEC monomer. f, The overlay of the NADPH-binding pockets in HEC and EasCCf. Dashed lines indicate polar interactions with distance <3.5 Å. g, Sequence alignment between the amino acids forming the NADPH binding pocket in HEC and EasCCf, which was performed with ClustalW using MEGA11 and visualized with ENDscript 3. The red boxes indicate the residues forming hydrogen bonding interactions with the bonded NADPH in HEC and their equivalents in EasCCf. See Supplementary Fig. 5 for a full sequence alignment between EasCCf and HEC.