Fig. 6: Crystal structure of mouse Tha1 improves HTML-OSMES results.

a Quaternary assembly of Tha1. The four PLP cofactors, one for each unit, are shown in violet ball-and-stick. The main interface, between units A and B (orange/magenta) and the secondary interface between units C and D (teal/pale cyan) are indicated. b Active site of Tha1. The main polar interactions of the PLP cofactor (violet) at the interface between subunits A (carbon atoms in teal) and B (carbon atoms in pale cyan) are indicated. Distances in Å. c Comparison of AlphaFold model (dark colors) and the Tha1 crystal structure (orthorhombic F222, light colors) docked with HTML-PLP substrate. Different chains are colored in different colors. Non-carbon atoms are colored according to CPK convention. HTML-PLP and flexible catalytic lysine are shown in ball-and-sticks. The binding site residues (≤4.5 Å from HTML-PLP) are shown in sticks. Polar interactions are indicated with orange dashes, cation-π interactions are indicated with olive dashes; residues showing a different position in the model and crystallographic structure are labeled. Clustering of the HTML-PLP conformations at the Tha1 active site obtained with HTML-OSMES applied to AlphaFold model (d, e) or the crystal structure (f, g). Bar plots show the distribution of χ₁ (blue), χ₂ (emerald) and χ₃ (kiwi) angles in each cluster, with the catalytic cluster highlighted in light blue. Circular plots show the cumulative distribution of the three χ angles for all clusters. |sin(χ)| ≥0.95 values are defined by gray areas. Source data are provided as a Source Data file.