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Figure 2.
Figure 2. Comparison of mouse ADH2 subunit A (orange) with
horse liver ADH1 apo (green) and holo (blue) subunits. C^a
chains of the individual coenzyme-binding domains are
superpositioned. Coenzyme-binding domains are to the left and
the catalytic domains to the right. Zinc atoms and NADH are
depicted in purple and brown, respectively. The three structural
segments with insertions, deletions and high rms deviations as
compared to other ADH structures are colored red and denoted
V1-V3 (V1, residues 55-61; V2, residues 114-121; V3, residues
294-307). The mouse ADH2 A-subunit is semi-open about half way
between the open apo and the closed holo form of horse liver
ADH1.
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