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EC Number Crystallization (Commentary) Reference
Display the word mapDisplay the reaction diagram Show all sequences 4.2.2.8isoform Hep III, to 2.2 A resolution. The enzyme comprises an N-terminal alpha/alpha-barrel domain and a C-terminal antiparallel beta-sheet domain as its basic scaffold. Isoform Hep III exhibits an open form compared with the closed form of Hep II. An active site of Hep III is located in the deep cleft at the interface between its two domains 729269
Display the word mapDisplay the reaction diagram Show all sequences 4.2.2.8isoform HepIII, to 1.6 A resolution. The overall architecture of HepIII belongs to the (alpha/alpha)5 toroid subclass with an N-terminal toroid-like domain and a C-terminal beta-sandwich domain. An elimination mechanism is suggested whereby Asn260 and His464 neutralize the carboxylic group, whereas Tyr314 serves both as a general base in C-5 proton abstraction, and a general acid in a proton donation to reconstitute the terminal hydroxyl group, respectively 730858
Display the word mapDisplay the reaction diagram Show all sequences 4.2.2.8structures of two crystal forms at resolution 1.8 and 2.4 A. Tyr301 is the main catalytic residue 747916
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