Literature summary for 1.14.14.47 extracted from

Holden, J.K.; Kang, S.; Hollingsworth, S.A.; Li, H.; Lim, N.; Chen, S.; Huang, H.; Xue, F.; Tang, W.; Silverman, R.B.; Poulos, T.L.
Structure-based design of bacterial nitric oxide synthase inhibitors (2015), J. Med. Chem., 58, 994-1004.

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Cloned(Commentary)

Cloned (Comment)	Organism
-	Bacillus subtilis

Crystallization (Commentary)

Crystallization (Comment)	Organism
in complex with inhibitors that target both the active and pterin sites	Bacillus subtilis

Inhibitors

Inhibitors	Comment	Organism	Structure
6,6'-[(5-amino-1,3-phenylene)di(ethane-2,1-diyl)]bis(4-methylpyridin-2-amine)	compound interacts with the active site Glu243 and heme propionate D through a series of hydrogen bonds between the aminopyridine functional groups. Comparison with inhibition of mammalian NOS isoforms	Bacillus subtilis
6,6'-[[5-(aminomethyl)-1,3-phenylene]di(ethane-2,1-diyl)]bis(4-methylpyridin-2-amine)	compound interacts with the active site Glu243 and heme propionate D through a series of hydrogen bonds between the aminopyridine functional groups. Comparison with inhibition of mammalian NOS isoforms	Bacillus subtilis

Organism

Organism	UniProt	Comment	Textmining
Bacillus subtilis	O34453	-	-
Bacillus subtilis 168	O34453	-	-

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Release 2023.1 (January 2023)