Literature summary for 3.6.1.61 extracted from

Zheng, Q.C.; Li, Z.S.; Sun, M.; Zhang, Y.; Sun, C.C.
Homology modeling and substrate binding study of Nudix hydrolase Ndx1 from Thermos thermophilus HB8 (2005), Biochem. Biophys. Res. Commun., 333, 881-887.

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Metals/Ions

Metals/Ions	Comment	Organism	Structure
Mg2+	homology modeling techniques shows that Ser38, Leu39 and Glu46, coordinate enzyme-bound Mg2+ ions in the complex of Ndx1 with P1,P6-bis(5'-adenosyl)hexaphosphate	Thermus thermophilus

Organism

Organism	UniProt	Comment	Textmining
Thermus thermophilus	-	-	-

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
additional information	homology modeling techniques shows Glu46, Arg88, and Glu90 are three important determinant residues in binding as they have strong hydrogen bonding interactions and electrostatic interactions with P1,P6-bis(5'-adenosyl)hexaphosphate	Thermus thermophilus	?	-	?

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Release 2023.1 (January 2023)