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Comparison of the oxyanion hole in hWE and mWE in the presence and absence of PAR1. Left, PAR1 binding in hWE (light green) induces rotation of the Glu-192—Gly-193 peptide bond such that the backbone O atom is in H-bonding distance of both the OH and backbone N atom of the catalytic Ser-195. Right, in all mWE structures the Glu-192—Gly-193 peptide bond is flipped whether free (wheat) or bound to the PAR1 peptide (light green).
