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EC Number General Information Commentary Reference
Display the word mapDisplay the reaction diagram Show all sequences 1.14.13.208more benzoyl-CoA substrate forms two hydrogen bonds with Gln116, which in turn is hydrogen-bonded to Glu120. A number of other second-shell residues are also important for the orientation of the benzoyl moiety, including Thr119, Ser123, Phe193, Phe203, and Thr210. Optimized structure of the BoxB active site with the truncated benzoyl-CoA and O2 substrates bound, corresponding to the Michaelis complex, enzyme structure and reaction mechanism mechanics/molecular mechanics calculations and modeling, overview 744692
Display the word mapDisplay the reaction diagram Show all sequences 1.14.13.208more usage of PDB ID 3PM5 for enzyme structure modeling and simulation, quantum mechanics/molecular mechanics calculations, overview. Four general pathways for oxidizing aromatic rings are determined -, 745167
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