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. Author manuscript; available in PMC: 2009 Nov 1.
Published in final edited form as: Amino Acids. 2008 Mar 28;35(4):719–730. doi: 10.1007/s00726-008-0062-5

Fig. 8.

Fig. 8

Structure P5CDH from T. thermophilus (Inagaki et al. 2006). A, ribbon drawing of a P5CDH subunit. The three domains are colored blue (NAD+-binding), green (catalytic) and pink (dimerization). The NAD+ cofactor is shown in yellow sticks. Catalytic Cys322 is represented in spheres. B, ribbon drawing of a P5CDH dimer. The two subunits of the dimer are colored as in panel A. C, close-up view of the intermolecular β-sheet in the dimer interface.

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