EC Number   |
Inhibitors |
Structure |
|---|
   2.1.1.228 | sinefungin |
an active-site inhibitor and S-adenosyl-L-methionine (SAM) analogue, that binds at the N-terminal dommain in the SAM binding site. Structure analysis of crystallized isolated dimeric NTD, overview |
   |
| 2.1.1.228 | sinefungin |
and isosteric SAM analogue in which the methyl group of SAM is replaced by an amino group and the sulfur by a carbon atom, competitive inhibition with respect to SAM and uncompetitive for tRNA. A set of crystal structures of the homodimeric PaTrmD protein bound to SAM and sinefungin provide the molecular basis for enzyme competitive inhibition and identify the location of the bound divalent ion. Crystal structure of PaTrmD bound to the SAM-competitive inhibitor sinefungin (SFG) is refined at a resolution of 2.45 A. In order to unambiguously locate the divalent ion, a third structure where crystals of PaTrmD are soaked with Mn2+ and SFG is determined. One Mn2+ near each of the bound sinefungin can be built. Mn2+ is coordinated by side-chain carbonyl group of E173', carboxylic groups of E121, D174' and D182' and the nitrogen atom of the sinefungin tail |
|
| 2.1.1.228 | suramin |
- |
|
| 2.1.1.228 | [4-(hydroxymethyl)-2,8-diazaspiro[4.5]decan-2-yl][1-(4-methoxyphenyl)cyclohexyl]methanone |
- |
|
| 2.1.1.228 | [5-(furan-2-yl)-4-oxo-3,4-dihydrothieno[2,3-d]pyrimidin-2-yl]methyl pyrazine-2-carboxylate |
- |
|
