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2.1.1.300
dimer
PavNMT forms a dimer with 2fold rotational symmetry in the asymmetric unit that is not seen in homologous NMTs
757162
2.1.1.300
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the overall structure of PavNMT reveals the presence of an alpha/beta SAM-binding domain with a canonical Rossmann fold that is shared among most SAM-dependent methyltransferases. In addition to this domain, a primarily alpha-helical BIA-binding domain forms the majority of the putative binding site for the methyl group acceptor
757162
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