Extended Data Fig. 5: The interface details and regulatory modes between the core enzyme Rpd3 and its neighboring subunits.

a. A global view of the interactions around the core enzyme Rpd3. The positions of interaction are marked with numbers. Detailed views of the interactions between Rpd3 and HID-N of Sin3, PHD1 of Rco1-A, Eaf3-A (b); LoopS of Sin3 (c); FHF of Sin3 (d); HID-C of Sin3 (e); αβC of Rco1-A (f); PHD2 of Rco1-A (g). Residues at the interface are depicted as sticks. h. Close-up view of interactions between the HID domain of Sin3 shown in cartoon and Rpd3 shown in surface representation. i. Comparison of the overall structure and key amino acids in the basic pocket of HDACs. Rpd3S is colored in blue, HDAC1 is colored in green, and HDAC3 is colored in purple. j. Structural comparison of HDAC complexes in inositol phosphates regulation. Rpd3S complex: Rpd3-Sin3, MiDAC complex: HDAC1-MIDEAS (PDB ID: 6Z2J)⁶², SMRT complex: HDAC3-SMRT (PDB ID: 4A69)²⁹, NuRD complex: HDAC1-MTA1 (PDB ID: 4BKX)²⁸. k. Sequence conservation analysis of the α2 of Sin3 from yeast to human.