Literature summary for 1.4.3.3 extracted from

Kohiki, T.; Kato, Y.; Nishikawa, Y.; Yorita, K.; Sagawa, I.; Denda, M.; Inokuma, T.; Shigenaga, A.; Fukui, K.; Otaka, A.
Elucidation of inhibitor-binding pockets of d-amino acid oxidase using docking simulation and N-sulfanylethylanilide-based labeling technology (2017), Org. Biomol. Chem., 15, 5289-5297 .

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Crystallization (Commentary)

Crystallization (Comment)	Organism
search for binding pockets of DAO to its inhibitor 4-bromo-3-nitrobenzoate by combining in silico docking simulation and labeling experiments employing an N-sulfanylethylanilide-based labeling technology. There are two binding pockets: one is shared with D-Ser and FAD, and the other is an cleft between the subunits of a DAO dimer	Homo sapiens

Inhibitors

Inhibitors	Comment	Organism	Structure
4-bromo-3-nitrobenzoate	there are two binding pockets of DAO to its inhibitor 4-bromo-3-nitrobenzoate, one is shared with substrate D-Ser and FAD, and the other is an cleft between the subunits of a DAO dimer	Homo sapiens

Organism

Organism	UniProt	Comment	Textmining
Homo sapiens	P14920	-	-

Cofactor

Cofactor	Comment	Organism	Structure
FAD	-	Homo sapiens

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Release 2023.1 (January 2023)