Literature summary extracted from

Rao, R.G.; Biswal, J.; Dhamodharan, P.; Kanagarajan, S.; Jeyaraman, J.
Identification of potential inhibitors for AIRS from de novo purine biosynthesis pathway through molecular modeling studies - a computational approach (2016), J. Biomol. Struct. Dyn., 34, 2199-2213 .

Crystallization (Commentary)

EC Number	Crystallization (Comment)	Organism
6.3.3.1	molecular modeling based on Escherichia coli crystal structure, and molecular dynamics simulation. The binding pocket is composed of residues Lys13, Thr14, Ala17, Leu18, Ile21, Arg26, Lys35, Glu38, Pro39, Glu40, Asp103, Leu105, Ile133, Gly135, Gly136, Gln137 and Thr138	Pyrococcus horikoshii

Inhibitors

EC Number	Inhibitors	Comment	Organism	Structure
6.3.3.1	(2R,3S,4R,5R)-2-(aminomethyl)-5-(hydroxymethyl)oxolane-3,4-diol	i.e. NCI_121957. Molecular docking, compound interacts with residues Lys35, Thr14, Gly136, Glu137 and Asp103, best inhibitor identified	Pyrococcus horikoshii

Organism

EC Number	Organism	UniProt	Comment	Textmining
6.3.3.1	Pyrococcus horikoshii	O58054	-	-
6.3.3.1	Pyrococcus horikoshii OT-3	O58054	-	-

Synonyms

EC Number	Synonyms	Comment	Organism
6.3.3.1	AIRS	-	Pyrococcus horikoshii
6.3.3.1	aminoimidazole ribonucleotide synthetase	-	Pyrococcus horikoshii
6.3.3.1	PurM	-	Pyrococcus horikoshii

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Release 2023.1 (January 2023)