[Conformation of threo-alpha-cycloglutamic acid and pyridoxal-5'-phosphate aldimine in the active site of aspartate aminotransferase].
The theoretical conformational analysis of the pyridoxal-5'-phosphate aldimine complex with a substrate analogue--threo-alpha-cycloglutamic acid has been carried out. The calculation method used takes into account the possibility of hydrogen bonding between a carboxyl group of the substrate and the phosphate moiety of the cofactor. The conformational properties and geometrical parameters of the lowest energy structures are discussed. It is shown that of the three conformations permitted for the productive enzyme--substrate complex formations only one is electrostatically favourable.
D001219:Aspartate Aminotransferases / Q000378:metabolism; D001665:Binding Sites; D008968:Molecular Conformation; D010080:Oxazoles; D011485:Protein Binding; D011487:Protein Conformation; D011732:Pyridoxal Phosphate / Q000031:analogs & derivatives*
D010080:Oxazoles; C006513:4-amino-5-carboxymethylisoxazolid-3-one; D011732:Pyridoxal Phosphate; D001219:Aspartate Aminotransferases
Konformatsiia al'dimina tgeo-al'ta-tsikloglutaminovoĭ kisloty i piridoksal'-5'-fosfata v aktivnom tsentre aspartat-transaminazy.