[The mobility of the side chains of His57 and other amino acid residues in the active center of chymotrypsin].
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Using the "hard-sphere" atom-atom approximation with consideration of the available X-ray data, the possibility of free rotation of the side chain of His57 residue in the active center of chymotrypsin was studied. It was shown that there is a significant rotational freedom of the imidazole ring on chi1 and chi2 torsional angles. The rotation is accompanied by the movement of the side chains of Tyr94, Ile99 and Ser195 residues. It was assumed that the four residues act as movable parts of the motor of the enzymatic machinery. Amino acid residues that contact the cavity around the His57 imidazole ring were identified.