Crystal structures of the selenoprotein glutathione peroxidase 4 in its apo form and in complex with the covalently bound inhibitor ML162

Moosmayer, D.; Hilpmann, A.; Hoffmann, J.; Schnirch, L.; Zimmermann, K.; Badock, V.; Furst, L.; Eaton, J.K.; Viswanathan, V.S.; Schreiber, S.L.; Gradl, S.; Hillig, R.C.

doi:10.1107/S2059798320016125

Acta Crystallographica Section D
Acta Crystallographica
Section D STRUCTURAL BIOLOGY

IUCr IT WDC

home archive editors for authors for readers submit subscribe open access

view article

Figure 4
Electron-density maps for GPX4^WT. (a) 2mF_o − DF_c map at the active site, contoured at 1.5σ, with the final GPX4^WT model shown in stick representation. Three residues of the catalytic tetrad are shown. The occupancy of the Se atom of Sec46 is 0.60. (b)–(e) show 2mF_o − DF_c maps (blue) contoured at 1.5σ after modeling residue 46 as cysteine (b) or as selenocysteine with different occupancies (c, d, e). Difference density (mF_o − DF_calc) maps are contoured at 3σ (green) and −3σ (red), respectively.

STRUCTURAL
BIOLOGY

ISSN: 2059-7983

Volume 77| Part 2| February 2021| Pages 237-248

https://doi.org/10.1107/S2059798320016125

Open

access

Follow Acta Cryst. D

Search IUCr Journals		doi		Advanced search
Author		volume	page