EC Number   |
Reference |
|---|
   1.11.1.12 | crystal structure of the selenocysteine 46 to cysteine mutant, residues Met1 to Leu170, to 1.8 A resolution |
741538 |
| 1.11.1.12 | molecular modeling of mutant C2S/C10S/C37S/C66S/C75S/C107S/C148S. The catalytic tetrad consists of residues Sec46, Gln81, Trp136, and Asn137 |
742558 |
| 1.11.1.12 | sparse matrix crystallization method, crystal structure of the catalytically active U46C mutant of human GPx4 to 1.55 A resolution |
685185 |
| 1.11.1.12 | structure of recombinant protein, at 1.3 A resolution. Data indicate a monomeric protein, which contains the catalytic selenium at the redox level of the seleninic acid. The presumed catalytic triad consists of residues Sec(Cys)46, Gln81 and Trp136. The triad is localized at a flat impression of the protein surface |
764227 |
| 1.11.1.12 | 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 |
763834 |
| 1.11.1.12 | the crystal structure is solved to a resolution of 2.0 A |
701118 |
| 1.11.1.12 | the crystal structures of the Sec43Cys and Sec43Ser mutants are solved at resolutions of 1.0 A and 1.7 A, respectively |
701138 |
