Aspartate aminotransferase Ramachandran plot

Figure 2-10 Ramachandran plot for cytosolic aspartate aminotransferase. The angles and / were determined experimentally from X-ray diffraction data at 0.16 nm resolution and model building. The majority of conformations are those of a helices or of P structure. Glycine residues are indicated by filled circles, while all other residues are denoted by an "x". One of these (green) lies quite far from an allowed area and must give rise to localized strain.104b Extreme lower limit "allowed" regions by the hard-sphere criteria are shown in outline. From coordinates of Arthur Amone et al. (unpublished).106...

$Figure 2-10 Ramachandran plot for cytosolic aspartate aminotransferase. The angles and / were determined experimentally from X-ray diffraction data at 0.16 nm resolution and model building. The majority of conformations are those of a helices or of P structure. Glycine residues are indicated by filled circles, while all other residues are denoted by an "x". One of these (green) lies quite far from an allowed area and must give rise to localized strain.104b Extreme lower limit "allowed" regions by the hard-sphere criteria are shown in outline. From coordinates of Arthur Amone et al. (unpublished).106...$

Aspartate aminotransferase 57s, 135s, 753 absorption spectra 749 active site structure 744 atomic structure 750 catalytic intermediates, models 752 NMR spectra 149 quinonoid intermediate 750 Ramachandran plot 61 sequence 57 transamination 742 Aspartate ammonia-lyase 685 Aspartate carbamoyltransferase 348s active sites 348 regulation 540... [Pg.907]

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