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Literature summary for 1.11.1.12 extracted from

  • Moosmayer, D.; Hilpmann, A.; Hoffmann, J.; Schnirch, L.; Zimmermann, K.; Badock, V.; Furst, L.; Eaton, J.; Viswanathan, V.; Schreiber, S.; Gradl, S.; Hillig, R.
    Crystal structures of the selenoprotein glutathione peroxidase 4 in its apo form and in complex with the covalently bound inhibitor ML162 (2021), Acta Crystallogr. D Struct. Biol., 77, 237-248 .
    View publication on PubMedView publication on EuropePMC
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Cloned(Commentary)

Cloned (Comment) Organism
expression in HEK293-6E cell Homo sapiens

Crystallization (Commentary)

Crystallization (Comment) Organism
structure of the wild-type form of GPX4 at 1.0 A resolution and in complex with inhibitor 2-chloro-N-(3-chloro-4-methoxyphenyl)-N-[(1S)-2-(phenylethylethylamino)-2-oxo-1-(thiophen-2-yl)ethyl]acetamide. Active site residue is Sec46 Homo sapiens

Protein Variants

Protein Variants Comment Organism
C66S mutation of the second reactive Cys residue, crystallization data Homo sapiens

Inhibitors

Inhibitors Comment Organism Structure
2-chloro-N-(3-chloro-4-methoxyphenyl)-N-[(1S)-2-(phenylethylethylamino)-2-oxo-1-(thiophen-2-yl)ethyl]acetamide i.e. ML162 Homo sapiens

Organism

Organism UniProt Comment Textmining
Homo sapiens P36969 isoform Gpx4
-

Synonyms

Synonyms Comment Organism
GPx4
-
 Homo sapiens