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An overlay of the structure of WT thrombin (wheat) with a representative structure of the excited state (blue) showing rearrangement of the catalytic triad residues His57 (His79) and Ser195 (Ser241). The H-bond distance between the His and the Ser has increased from 2.9 to 3.9 Å, and Ser195 is now apparently occupying the oxyanion hole. To see this figure in color, go online.
