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

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Figure 9
Comparison with the binding site of a known peptide inhibitor. The structure of GPX4^C66S–(S)-ML162 is shown superimposed onto that of GPX4^U46C bound to a peptidic inhibitor (PDB entry 5h5s). For clarity only the peptide is shown for the latter, depicted with green C atoms. GPX4 is shown in surface representation, with the inhibitor (S)-ML162 with yellow C atoms, the surface of Sec46 colored red and the remaining residues of the catalytic triad in blue (Gln81), dark blue (Trp136) and purple (Asn137). (a) and (b) show two different orientations.

STRUCTURAL
BIOLOGY

ISSN: 2059-7983

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

https://doi.org/10.1107/S2059798320016125

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