Diphthine synthase

spinqualitylabelsall models Diphthine synthase complex with S-adenosyl-L-homocysteine (SAH) and Na+ ion 2owu Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Diphthine synthase (DPS) is a S-adenosyl-L-methionine (SAM)-dependent methyltransferase. DPS catalyzes the trimethylation of a specific histidine residue in elongation factor 2 forming a diphthine and producing S-adenosyl-L-homocysteine (SAH). DPS participates in the diphthamide biosynthesis. SAH binding site. Na coordination site (2owu), water molecules shown as red spheres.

3D structures of diphthine synthase

Updated on 15-July-2020

2owu – DPS – Archaeoglobus fulgidus
2dsg, 2dsh, 2dsi, 2hr8, 2dv3, 2dv4, 2dv5, 2dv7, 2dxv, 2dxw, 2dxx, 2e07, 2e08, 2e15, 2e16, 2e17, 2e4n, 2e4r, 2e7r, 2ed3, 2ed5, 2eeq, 2owf, 2owg, 2owk, 2owu, 2owv, 2egb, 2z6r, 2egl, 2egs, 2eh2, 2eh4, 2eh5, 2ehc, 2ehl, 2ejj, 2ejk, 2p5c, 2p5f, 2p6d, 2p6i, 2p6k, 2ejz, 2ek2, 2ek3, 2ek4, 2ek7, 2eka, 2p6l, 2p9d, 2el0, 2el1, 2el2, 2el3, 2eld, 2ele, 2emr, 2emu, 2en5, 2eni, 2pb4, 2pb5, 2pb6, 2pca, 2pcg, 2pch, 2pci, 2pck, 2pcm – PhDPS (mutant) + SAH – Pyrococcus horikoshii
1vce - PhDPS + SAH
3i4t - DPS (mutant) – Entamoeba histolytica

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