Factor Xa: Difference between revisions
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Hydrogen bonds form between the carbonyl oxygen of Ser214 and the NH of the P1 (Arg 14) residue, the NH of | Hydrogen bonds form between the carbonyl oxygen of Ser214 and the NH of the P1 (Arg 14) residue, the NH of | ||
Trp215 and the carbonyl of P3 (Asp 113) and the carbonyl of Gly216 and the NH of P3 (Asp 113). These interactions are a general feature of chymotrypsin-like proteases and are critical for efficient substrate hydrolysis. | Trp215 and the carbonyl of P3 (Asp 113) and the carbonyl of Gly216 and the NH of P3 (Asp 113). These interactions are a general feature of chymotrypsin-like proteases and are critical for efficient substrate hydrolysis. | ||
The precise interactions of the P' side chains have not been defined. The P1' and P3' residues point in the same direction as a consequence of the beta sheet alignment of the substrate, so that the S1' and S3' sites overlap. The S1'/S3' sites are bounded by His57, the 60’s loop and the 40’s loop. The P2' residue points in the opposite direction and may interact with the 150’s loop. | |||
====Catalytic Triad==== | ====Catalytic Triad==== | ||
