Literature summary for 1.1.1.21 extracted from

Steuber, H.; Heine, A.; Klebe, G.
Structural and thermodynamic study on aldose reductase: nitro-substituted inhibitors with strong enthalpic binding contribution (2007), J. Mol. Biol., 368, 618-638.

Crystallization (Commentary)

Crystallization (Comment)	Organism
in complex with NADP+ and inhibitor 4-[3-(3-nitrophenyl)-1,2,4-oxadiazol-5-yl]butanoic acid, 1.43 A resolution. The inhibitor occupies the active site with its carboxylate head group located at the catalytic cavity. In complex with inhibitor {[5-(5-nitrofuran-2-yl)-1,3,4-oxadiazol-2-yl]sulfanyl}acetic acid at 1.55 A resolution. The nitro-aromatic moiety of both inhibitors occupies the specificity pocket of the enzyme, binding to the bottom of the pocket and provoking remarkable induced-fit adaptations	Homo sapiens

Crystallization (Comment)

Organism

in complex with NADP+ and inhibitor 4-[3-(3-nitrophenyl)-1,2,4-oxadiazol-5-yl]butanoic acid, 1.43 A resolution. The inhibitor occupies the active site with its carboxylate head group located at the catalytic cavity. In complex with inhibitor {[5-(5-nitrofuran-2-yl)-1,3,4-oxadiazol-2-yl]sulfanyl}acetic acid at 1.55 A resolution. The nitro-aromatic moiety of both inhibitors occupies the specificity pocket of the enzyme, binding to the bottom of the pocket and provoking remarkable induced-fit adaptations

Homo sapiens

Inhibitors

Inhibitors	Comment	Organism	Structure
4-[3-(3-nitrophenyl)-1,2,4-oxadiazol-5-yl]butanoic acid	crystallization data	Homo sapiens

Organism

Organism	UniProt	Comment	Textmining
Homo sapiens	P15121	isoform ALR2	-

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Release 2023.1 (January 2023)