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EC Number Crystallization (Commentary)
Display the word mapDisplay the reaction diagram Show all sequences 1.13.11.92structure to 1.5 A resolution. The structure is monomeric, predominantly helical-helical, and comprised of two domains. Helices H2, H6, H8, and H17 form the heme binding cleft and walls of the active site channel. Residues His318, Thr323, and Arg566 are located near the catalytic tyrosine, Tyr386, at the apex of the channel, where they interact with a chloride ion. Two extended inserts are present on the surface of the enzyme that restrict access to the distal face of the heme
Display the word mapDisplay the reaction diagram Show all sequences 1.13.11.92structures of wild-type in complex with H2O2, and the catalytically inactive Y379F mutant in complex with palmitic acid. PA binds within the active site cleft of alpha-DOX such that the carboxylate forms ionic interactions with residues His311 and Arg559. Thr316 aids in the positioning of carbon-2 for hydrogen abstraction. The binding of H2O2 at the distal face of the heme displaces residues His157, Asp158, and Trp159 about 2.5 A from their positions in the wild type structure
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