EC Number   |
Reference |
|---|
    2.6.1.13 | - |
637099, 637105, 637111, 637121, 637122, 637123, 637124, 637137 |
| 2.6.1.13 | complexed to gabaculine and L-canaline, hanging drop vapor diffusion method |
637138 |
| 2.6.1.13 | complexed with 5-fluoromethylornithine, hanging drop vapor diffusion method |
637140 |
| 2.6.1.13 | crystal structure analysis |
758876 |
| 2.6.1.13 | hanging drop vapor diffusion method |
637116, 637139 |
| 2.6.1.13 | homology modeling of crystal structure and flexible docking studies. G106 and K256 are the important residues in binding |
688463 |
| 2.6.1.13 | human OAT is crystallized as a recombinant protein obtained by expression of the entire gene in Escherichia coli, the packing of the dimers in the crystal yields a hexameric quaternary structure in which 3 dimers are arranged to form about one turn of a right-handed superhelix, OAT is also crystallized in the presence of L-canaline and gabaculine, co-crystallization of OAT with (2S, 5S)-5-fluoromethylornithine |
706356 |
| 2.6.1.13 | the three-dimensional crystal structure of Plasmodium falciparum OAT at 2.3 A resolution is reported. The overall structure is very similar to that of the human OAT. In plasmodial OAT, the loop involved in substrate binding contains two cysteine residues, which are lacking in human OAT |
722970 |
