EC Number   |
|---|
    6.3.4.13 | native enzyme and in complex with ATP, to 2.4 and 1.8 A resolution, respectively. Comparison of crystal structures of GAR-syn from Thermus thermophilus, Geobacillus kaustophilus and Aquifex aeolicus. The orientations of the B domains are varied among GAR-syns and the molecular dynamics simulation suggests the mobility of the B domain. The B loop in the B domain fixes the position of the beta- and gamma-phosphate groups of the bound ATP |
| 6.3.4.13 | native enzyme and in complex with phosphate, with AMP and phosphate, and with AMP and glycine, to 2.21, 2.20, 1.9 and 2.21 A resolution, respectively. Comparison of crystal structures of GAR-syn from Thermus thermophilus, Geobacillus kaustophilus and Aquifex aeolicus. The orientations of the B domains are varied among GAR-syn's and the molecular dynamics simulation suggests the mobility of the B domain. The B loop in the B domain fixes the position of the beta- and gamma-phosphate groups of the bound ATP |
| 6.3.4.13 | selenomethionine derivative, to 2.8 A resolution. Comparison of crystal structures of GAR-syn from Thermus thermophilus, Geobacillus kaustophilus and Aquifex aeolicus. The orientations of the B domains are varied among GAR-syns and the molecular dynamics simulation suggests the mobility of the B domain. The B loop in the B domain fixes the position of the beta- and gamma-phosphate groups of the bound ATP |
| 6.3.4.13 | selenomethionine incorporated enzyme, hanging drop vapor diffusion method |
