D-Glu hydrolysis in the active site of the AmicoTA, a transaminase from the Gram-negative mesophilic bacterium Aminobacterium colombiense

<p>500 frames from the QM(PBE0-D3/6-31G**)/MM molecular dynamic trajectory in the transition state region. The external potential is centered at 3.9&nbsp;&Aring; of the collective variable (a sum of the distances between the hydrogen atom of the protonated amino group and an oxygen atom the &alpha;-carboxylate group of the substrate and between the nitrogen atom of the substrate and a C4&acute; atom of PLP).</p> <p>In the PDB file the QM atoms have&nbsp; beta=1 and MM&nbsp;beta=0.</p>