EC Number   |
Reference |
|---|
   1.13.12.24 | hanging drop vapor diffusion method at 20°C, crystal structures of the apoAequorin complexes with the chiral deaza-analogs (S)-daCTZ and (S)-HM-daCTZ are determined, suggesting that the hydroxy moiety at the C6-hydroxyphenyl group and the carbonyl moiety of the imidazopyrazinone ring in coelenterazine are essential to bind the apoAequorin molecule through hydrogen bonding |
765663 |
| 1.13.12.24 | recombinantly expressed in Escherichia coli with Hexa-His-tag tail at N-terminal |
764867 |
| 1.13.12.24 | sitting drop vapor diffusion method, crystal structure of Cd2+-loaded apo-mnemiopsin1 at 2.15 A resolution. The structure reveals that mnemiopsin1 has a two-domain fold with four alpha-helices in each domain |
765058 |
| 1.13.12.24 | to 1.7 A resolution. A calcium ion is observed in each of the three EF-hand loops that have the canonical calcium-binding sequence, and each is coordinated in the characteristic pentagonal bipyramidal configuration. The calcium-loaded apo-protein retains the same compact scaffold and overall fold as the unreacted photoprotein containing the bound substrate, 2-hydroperoxycoelenterazine |
746389 |
| 1.13.12.24 | to 1.7 A resolution. A calcium ion is observed in each of the three EF-hand loops that have the canonical calcium-binding sequence, and each is coordinated in the characteristic pentagonal bipyramidal configuration. The calcium-loaded apo-protein retains the same compact scaffold and overall fold as the unreacted photoprotein containing the bound substrate, 2-hydroperoxycoelenterazine and also the same as the Ca2+-discharged obelin bound with the product, coelenteramide |
746389 |
| 1.13.12.24 | to 2.3 A resolution. Aequorin is a globular molecule containing a hydrophobic core cavity that accommodates the ligand coelenterazine-2-hydroperoxide |
745878 |
