Stereo molecular diagrams

Fig. 6.16 Stereo packing diagrams of the low temperature yellow (upper) and the high temperature red (lower) forms of 6-XXX. In both cases the view is on the best molecular plane, which is approximately along the c axis, measuring 8.44 A in the yellow form and 6.99 A in the red form. Large circles depict the Pd atoms.

Figure 3.12 The enzyme lysozyme viewed to illustrate the active site cleft, (a) Skeletal diagrams in stereo (kindly prepared by Dr J. Rafteiy). (b) Beevers molecular model (with permission to be reproduced here), (c) Schematic of the alternating NAG-NAM substrate and the bond cleaved, catalysed by the enzymatic residues asp 52 and glu 35. Based on the coordinates of Diamond (1974).

Fig. 14.13. Stereo diagram of the C° trace of a tetramer of 3a,20 8-HSD with three molecular noncrystallographic twofold axes P, Q, and R. The subunit colors yellow, green, blue, and red are to be identified with subunit names A, B, C, and D, respectively. Four NAD(H) molecules are shown in pink. Also shown in the figure are two modeled cortisone molecules in catalytic clefts of the yellow and green subunits. These clefts are exposed to the top surface of the tetramer. T vo other cortisone molecules in clefts exposed to the bottom surface are not shown...

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