EC Number   |
|---|
   2.1.1.375 | domain VI of the VSV L protein contains a 2'-O-ribose methyltransferase (MTase) domain. Structural homology model of residues 1644-1842 within domain VI. The binding pocket consists of seven beta-strands and six alpha-helices. Highly conserved glycines are lining the interior of the pocket. Conserved aspartic acid D1762 is positioned at the perimeter of the pocket and interacts with invariantly conserved residues K1651, K1795, and E1833 to constitute the catalytic tetrad |
| 2.1.1.375 | structure of rabies virus L protein bound with its phosphoprotein cofactor, at 3.3 A resolution. In the methyltransferase domain, a shared GxGxG motif forms the binding site for the methyl donor, S-adenosylmethionine, and a conserved set of charged residues Lys1685, Asp1797, Lys1829, and Glu1867 forms the catalytic tetrad |
| 2.1.1.375 | the multifunctional large polymerase protein L is organized L into a ring domain containing the RNA polymerase and an appendage of three globular domains containing the cap-forming activities. The capping enzyme maps to a globular domain, which is juxtaposed to the ring, and the cap methyltransferase maps to a more distal and flexibly connected globule. Upon viral phosphoprotein binding, L undergoes a significant rearrangement |
