Comparisons of crystal structure and AlphaFold 3 models of KatASS1. (A) Overlay of crystal structure KatASS1 (two chains, yellow) and crystal structures of KatA26659 (light gray, four chains). Variant sites are noted in pink. (B–E) Poses of variant residues within KatASS1, as indicated. KatASS1 crystal structure chains are shown in yellow and KatA26995 crystal structure chains in light gray. Green mesh is mFo-DFc omit map electron density at 3.5 σ averaged over the two non-crystallographic symmetry (NCS) chains, and dark blue mesh is 2mFo-DFc NCS-averaged electron density at 1.0 σ of the final model. (F) Overlay of the KatASS1 crystal structure (yellow) with three AlphaFold 3 models (light blue, blue, and dark blue) using native sequence and tetramer oligomerization as input parameters. (G–J). Overlay of each variant residue comparing crystal structure (yellow) positions to AlphaFold three predictions (blue). (K). Global root-mean-square-deviation (RMSD) values for each structure and model in relation to crystal structure KatASS1 chain A.
Wonderful how Alphafold has opened up protein structure prediction to non-experts but you still have to feed it correct information (like oligomeric state!). A small test case shows AF3 makes excellent guesses on natural variants but inaccuracies occur from dubious user inputs.
#microsky #IDsky 🧪🦠