2.1.1.244	dimer	2 * 33000, recombinant isozyme NRMT1, SDS-PAGE and analytical ultracentrifugation	
2.1.1.244	additional information	NRMT lacks a SET domain but possesses a Rossman-like alpha/beta fold	
2.1.1.244	additional information	the enzyme is a seven beta-strand methyltransferase	
2.1.1.244	additional information	the structure of enzyme NTMT1 includes a typical methyltransferase Rossmann fold that consists of a seven-strand beta sheet and five alpha helixes, of which two alpha helixes (alpha6 and alpha7) pack on one side of the beta sheet, and the other three alpha helixes (alpha3, alpha4, and alpha5) pack on the other side of the beta sheet. In addition to the highly conserved Rossmann fold, enzyme NTMT1contains two unique structural elements distinct from other methyltransferases: a beta hairpin inserted between strand beta5 and helix alpha7 and an N-terminal extension consisting of two alpha helixes (alpha1 and alpha2) and one 310 helix. These two unique structural elements are extensively involved in substrate binding, suggesting their potential contributions to substrate specificity	
2.1.1.244	additional information	isozyme NRMT1 primarily exists as a dimer. Isozymes NRMT1 and NRMT2, when co-expressed, form a heterotrimer, interaction analysis, overview. When NRMT2 monomer is present the NRMT1 dimer will bind it and the pool of NRMT1 dimer is completely depleted