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EC Number Crystallization (Commentary)
Display the word mapDisplay the reaction diagram Show all sequences 2.1.1.369ATXR5 contains a bipartite catalytic domain composed of nSET and SET. The selectivity pocket and safety belt of ATXR5/6-type H3K27 methyltransferases are responsible for H3.1 preference over H3.3
Display the word mapDisplay the reaction diagram Show all sequences 2.1.1.369structure of PCNA in complex with ATXR6 PIP motif
Display the word mapDisplay the reaction diagram Show all sequences 2.1.1.369structure of the PHD domain (residues 23-77) bound to the unmodified histone H3 tail. The domain adopts a canonical crossbraced PHD domain architecture with two loops containing the Cys4-His-Cys3 motif that coordinates two zinc atoms, a double-stranded twisted antiparallel beta-sheet and two short 310 alpha-helices
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