English: Figure 2 (A) Stereo view of AT in standard orientation with the handles of the basket at the top of the model. The different modules are depicted in different colours (modules I, II, III, IV and V are presented in purple, blue, green, yellow and orange, respectively; the C-terminal -strand completing module I is shown in red) and the active site cysteine residue is shown in a ball-and-stick representation. Helices are numbered with Hn, strands with Sn. The secondary structure elements were determined with the program DSSP (Kabsch and Sander, 1983) and the figure was produced with MOLSCRIPT (Kraulis, 1991). (B) Stereo view of the AT model from the bottom of the basket, revealing the 5-fold pseudosymmetry of the model. The figure was designed with MOLSCRIPT (Kraulis, 1991), the colours are the same as in (A).
Andreas Humm, Erich Fritsche, Stefan Steinbacher and Robert Huber; Crystal structure and mechanism of human L-arginine:glycine amidinotransferase: a mitochondrial enzyme involved in creatine biosynthesis; The EMBO Journal (1997) 16, 3373–3385, doi:10.1093/emboj/16.12.3373
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2007-04-30 19:06 Adnanie 484×582× (67669 bytes) Figure 2 (A) Stereo view of AT in standard orientation with the handles of the basket at the top of the model. The different modules are depicted in different colours (modules I, II, III, IV and V are presented in purple, blue, green, yellow and orange, r
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{{Information |Description={{en|Figure 2 (A) Stereo view of AT in standard orientation with the handles of the basket at the top of the model. The different modules are depicted in different colours (modules I, II, III, IV and V are presented in purple...