EC Number   |
|---|
    4.1.1.50 | - |
| 4.1.1.50 | AdoMetDC F223A mutant complexed with S-adenosylmethionine and the wild type protein complexed with several substituted inhibitors, hanging drop vapor diffusion method, at 22°C in 13-16% PEG 8000, 100 mM Tris, pH 8.0-9.0, and 10 mM dithiothreitol |
| 4.1.1.50 | cocrystallized with 5'-deoxy-5'-dimethylthioadenosine and 5'-deoxy-5'-(N-dimethyl)amino-8-methyladenosine, hanging drop vapor diffusion method, at 22°C in 13-16% (w/v) polyethylene glycol 8000, 100 mM tris(hydroxymethyl)aminomethane (pH 8.0-9.0), and 10 mM dithiothreitol |
| 4.1.1.50 | docking of inhibitor 2-amino-3-[(E)-(2-fluorophenyl)diazenyl]-4,5,6,7-tetrahydro-8H-cyclopenta[d]pyrazolo[1,5-a]pyrimidin-8-one, compound binds the enzyme with interactions similar to known inhibitors. The major interactions are the ring-ring stacking interactions with Phe7 and Phe223, the polar interactions with the side-chain or main-chain atoms of Leu65, Ser68, Glu67, Asn224, and Cys226 |
| 4.1.1.50 | hanging drop vapour diffusion method, structures of the wild-type proenzyme and the S63A mutant at 1.55 A and 1.7 A resolution |
| 4.1.1.50 | in complex with different inhibitors and with a substrate analogue |
| 4.1.1.50 | in complexes with S-adenosylmethionine methyl ester and 5'-deoxy-5'-dimethylthioadenosine, hanging drop vapor diffusion method, using 2.4-2.8 M ammonium formate and 100 mM HEPES pH 8.0 |
| 4.1.1.50 | molecular modeling using enzymes from Solanum tuberosum and Homo sapiens as templates |
| 4.1.1.50 | structure of proenzyme in complex with putrescine and inhibitor N4-(3,5-dibromophenyl)-6-methylpyrimidine-2,4-diamine |
