Literature summary for 1.1.1.21 extracted from

Sekhon, G.; Singh, B.; Singh, R.
Role of Cys-298 in specific recognition of glutathione by aldose reductase (2021), J. Biomol. Struct. Dyn., FEHLT, 1-9 .

Crystallization (Commentary)

Crystallization (Comment)	Organism
molecular docking of glutathione analog gamma-glutamyl-S-(1,2-di-carboxyethyl)-cysteinyl-glycine, into the binding pocket of aldose reductase. Backbone nitrogens of residues Ala299 and Leu300 form a tiny pocket gated by the thiol group of Cys298. The glycine moiety of gamma-glutamyl-S-(1,2-di-carboxyethyl)-cysteinyl-glycine is able to displace the thiol group of Cys298 to make hydrogen bond interactions with the backbone of Ala299, Leu300, and Leu301	Homo sapiens

Crystallization (Comment)

Organism

molecular docking of glutathione analog gamma-glutamyl-S-(1,2-di-carboxyethyl)-cysteinyl-glycine, into the binding pocket of aldose reductase. Backbone nitrogens of residues Ala299 and Leu300 form a tiny pocket gated by the thiol group of Cys298. The glycine moiety of gamma-glutamyl-S-(1,2-di-carboxyethyl)-cysteinyl-glycine is able to displace the thiol group of Cys298 to make hydrogen bond interactions with the backbone of Ala299, Leu300, and Leu301

Homo sapiens

Organism

Organism	UniProt	Comment	Textmining
Homo sapiens	-	-	-

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Release 2023.1 (January 2023)