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LeuA allosteric (dimerization) domain This is the C-terminal regulatory (R) domain of alpha-isopropylmalate synthase, which catalyzes the first committed step in the leucine biosynthetic pathway. This domain, is an internally duplicated structure with a novel fold. It comprises two similar units that are arranged such that the two -helices pack together in the centre, crossing at an angle of 34 degrees, sandwiched between the two three-stranded, antiparallel beta-sheets. The overall domain is thus constructed as a beta-alpha-beta three-layer sandwich.
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Jiyao W et al.(2023). "The conserved domain database in 2023.",