Electronic structure calculations of HADHA and SOX9

This dataset consists of two parts:Part 1: In previous experiments, we found that acetylation at the K728 site of HADHA may affect its enzymatic activity. To further elucidate this finding from a structural perspective, we performed molecular docking simulations of the wild-type HADHA, the K728R mutant, and the HADHA K728ac mutant with their catalytic substrates, β-hydroxybutyryl-CoA. We calculated the Solvent Accessible Surface Area (SASA) and binding energies for all three forms of HADHA.Part 2: In earlier experiments, we discovered that the phosphorylation of six sites (T25, T87, S98, S136, T138, and T193) on the SOX9 protein could influence its interaction with the E3 ligase TRIM9, potentially affecting its ubiquitination and subsequent degradation. Therefore, we conducted molecular docking simulations to study the interactions between both the phosphorylated and non-phosphorylated forms of SOX9 and TRIM9.