EC Number   |
Cofactor |
Reference |
|---|
   2.1.1.228 | S-adenosyl-L-methionine |
- |
720240, 721026, 721035, 735421, 736428, 737226, 737228, 755697, 755960, 756152, 756161, 756163, 756631, 756774, 757201, 757408, 757409, 757582, 757790, 758324, 758348, 758376 |
| 2.1.1.228 | S-adenosyl-L-methionine |
binding structure analysis at 2.16 A resolution. PaTrmD shares functionally important amino acid residues involved in cofactor binding (Ser93-Gly96, Gly118, Ile123, Ser137, Gly145), tRNA binding (Gly60, Gly64, Ser203-His206) and catalytic activity (Asp54, Arg159, and Asp174) |
758329 |
| 2.1.1.228 | S-adenosyl-L-methionine |
dependent on |
735927, 737174 |
| 2.1.1.228 | S-adenosyl-L-methionine |
SAM |
756153 |
| 2.1.1.228 | S-adenosyl-L-methionine |
the AdoMet binding pocket is located between E206, R209, N380, P382, Y198 and R165. Due to the flexibility of D1 domain, a structure model is projected using only D2 and D3 domains, using structure PDB 2YX1 of chain A of Trm5 from Methanococcus jannashii as template |
757863 |
| 2.1.1.228 | S-adenosyl-L-methionine |
Trm5 binding structure, detailed overview |
721029 |
| 2.1.1.228 | S-adenosyl-L-methionine |
TrmD binding structure, detailed overview |
721029 |
