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Atomistry » Magnesium » PDB 7xqy-7y7s » 7xw8 » |
Magnesium in PDB 7xw8: Crystal Structure of Lysine Specific Demethylase 1 (LSD1) with Tak-418 Distomer, Fad-AdductEnzymatic activity of Crystal Structure of Lysine Specific Demethylase 1 (LSD1) with Tak-418 Distomer, Fad-Adduct
All present enzymatic activity of Crystal Structure of Lysine Specific Demethylase 1 (LSD1) with Tak-418 Distomer, Fad-Adduct:
1.14.99.66; Protein crystallography data
The structure of Crystal Structure of Lysine Specific Demethylase 1 (LSD1) with Tak-418 Distomer, Fad-Adduct, PDB code: 7xw8
was solved by
H.Oki,
with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:
Magnesium Binding Sites:
The binding sites of Magnesium atom in the Crystal Structure of Lysine Specific Demethylase 1 (LSD1) with Tak-418 Distomer, Fad-Adduct
(pdb code 7xw8). This binding sites where shown within
5.0 Angstroms radius around Magnesium atom.
In total 2 binding sites of Magnesium where determined in the Crystal Structure of Lysine Specific Demethylase 1 (LSD1) with Tak-418 Distomer, Fad-Adduct, PDB code: 7xw8: Jump to Magnesium binding site number: 1; 2; Magnesium binding site 1 out of 2 in 7xw8Go back to Magnesium Binding Sites List in 7xw8
Magnesium binding site 1 out
of 2 in the Crystal Structure of Lysine Specific Demethylase 1 (LSD1) with Tak-418 Distomer, Fad-Adduct
Mono view Stereo pair view
Magnesium binding site 2 out of 2 in 7xw8Go back to Magnesium Binding Sites List in 7xw8
Magnesium binding site 2 out
of 2 in the Crystal Structure of Lysine Specific Demethylase 1 (LSD1) with Tak-418 Distomer, Fad-Adduct
Mono view Stereo pair view
Reference:
Y.Hattori,
S.Matsumoto,
S.Morimoto,
M.Daini,
M.Toyofuku,
S.Matsuda,
R.Baba,
K.Murakami,
M.Iwatani,
H.Oki,
S.Iwasaki,
K.Matsumiya,
Y.Tominari,
H.Kimura,
M.Ito.
Design, Synthesis, and Structure-Activity Relationship of Tak-418 and Its Derivatives As A Novel Series of LSD1 Inhibitors with Lowered Risk of Hematological Side Effects. Eur.J.Med.Chem. V. 239 14522 2022.
Page generated: Thu Oct 3 13:24:14 2024
ISSN: ISSN 0223-5234 PubMed: 35749987 DOI: 10.1016/J.EJMECH.2022.114522 |
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