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 5
Comparison of wild-type GPX4 with previous GPX4 crystal structures. (a) Overall fold of GPX4^WT (PDB entry 6hn3), GPX4^U46C (PDB entry 2obi) and a mutant version of GPX4 in which position Sec46 was found to be oxidized to seleninic acid and all other cysteine residues were mutated to serine or alanine (PDB entry 6elw). Only the active-site residue Sec46/Cys46 is shown in stick representation for orientation. (b) View into the active site of GPX4. Residues lining the site around Sec46 are shown in stick representation and include the residues which form the catalytic tetrad (Sec46, Gln81, Trp136 and Asn137).

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