huMTAP | – | – | T18a
| – | – |
–
| P69b
| – | – | A94a
| C95b
| G96b
| F177 | I194b
| N195b
| M196 | T197a
| T219 | D220 | D222 | – | – | V231b
| V233 | V236 | – | – | – |
Li MTAP | G16 | G17 | – | R60 | H61 | H65 | P69 | I92 | N93 | A94 | – | – | F181 | – | G199 | M200 | T201 | – | – | – | M221 | M243 | – | – | – | – | V247 | – |
Tb MTAP | – | G18 | – | – | H62 | H66 | – | V93 | N94 | A95 |
–
| – |
–
| – | – | M204 | – | – | – | – | A225 | M247 | – | – | – | N250 | V251 | V254 |
MEME motifs | 5 | 5 | – | 2 | 2 | 2 | 2 | 3 | 3 | 3 | 3 | 3 | 1 | 1 | 1 | 1 | 1 | 1 | 1 | 1 | 1 | 4 | – | – | – | 4 | 4 | 4 |
- The table illustrates interacting residues (IRs) with MTA at a distance lower than or equal to a cutoff of 4Ǻ. Residues listed in the same column are structurally aligned IRs. As we did not dock the cofactor on the proteins, it was expected not to observe interactions on huMTAP involving the cofactor binding sites (R60, H61, T93). However, three cofactor- binding sites (a) were here identified as IR with MTA. (b) Corresponds to residues here identified as IRs but not on the crystal structure of huMTAP