  1.5.1.B8 | dimer |
YpODH is composed of three domains. NADPH binds along a canonical GXGXXA loop within the N-terminal NAD(P)H-binding domain. This domain forms one half of the active site. The other half, and the proposed location for substrate binding, is formed by the catalytic domain. These domains are separated by a central cleft. Embedded within the catalytic domain is a third domain that forms a dimerization interface. The NAD(P)H-binding domain has a Rossmann-like fold. This domain contains twelve beta-strands, five alpha-helices, and one 310 helix. Helix G acts as a linker connecting the NAD(P)H-binding domain with the C-terminal, predominantly alpha-helical, domains, structure overview |
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