Electronic structure calculations of HADHA and SOX9

This dataset consists of two parts:<b>Part 1</b>: 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.<b>Part 2</b>: 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.

该数据集包含两部分：<b>第一部分</b>：在前期实验中，我们发现HADHA的K728位点乙酰化可能影响其酶活性。为从结构层面进一步阐明这一发现，我们对野生型HADHA、K728R突变体及HADHA K728ac突变体与其催化底物β-羟基丁酰辅酶A（β-hydroxybutyryl-CoA）进行了分子对接模拟。我们计算了这三种形式HADHA的溶剂可及表面积（Solvent Accessible Surface Area, SASA）及结合能。<b>第二部分</b>：在早期实验中，我们发现SOX9蛋白上六个位点（T25、T87、S98、S136、T138及T193）的磷酸化可能影响其与E3连接酶TRIM9的相互作用，进而潜在影响其泛素化及后续降解过程。因此，我们开展了分子对接模拟，以研究磷酸化与非磷酸化形式的SOX9蛋白与TRIM9之间的相互作用。