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Results 1 - 3 of 3
EC Number Subunits Commentary Reference
Display the word mapDisplay the reaction diagram Show all sequences 2.6.1.78? x * 43000, SDS-PAGE 722267
Display the word mapDisplay the reaction diagram Show all sequences 2.6.1.78homodimer AtPAT crystallizes as a homodimer. Each monomer of AtPAT consists of 15 alpha-helices and 9 beta-strands divided between two structural domains. The N-terminal domain (Lys115-Leu353) contains two sets of three a-helices surrounding six parallel and one anti-parallel beta-strand. Two additional alpha-helices in the PLP-binding pocket, as well as the a-helix connecting the N- and C-terminal domains, complete the N-terminal domain. The smaller C-terminal domain contains part of the N-terminal region (Ser71-Pro114) and residues Gly354 through Leu469, totaling five alpha-helices and two beta-strands. The N-terminal flexible loop (Ser71-Ser82) and features of the N-terminal domain form the dimer interface 759965
Display the word mapDisplay the reaction diagram Show all sequences 2.6.1.78tetramer 2 * 44000 + 2 * 57000, alpha2beta2-structure, SDS-PAGE 657636
Results 1 - 3 of 3