Literature summary for 4.2.1.10 extracted from

Iqbal, N.; Kumar, M.; Sharma, P.; Yadav, S.P.; Kaur, P.; Sharma, S.; Singh, T.P.
Binding studies and structure determination of the recombinantly produced type-II 3-dehydroquinate dehydratase from Acinetobacter baumannii (2017), Int. J. Biol. Macromol., 94, 459-465 .

Search for more literature for 4.2.1.10

Cloned(Commentary)

Cloned (Comment)	Organism
expression in Escherichia coli	Acinetobacter baumannii

Crystallization (Commentary)

Crystallization (Comment)	Organism
to 2.0 A resolution, monoclinic space group P21 with cell dimensions a = 82.3, b = 95.3, c = 132.3 A and beta = 95.7°. The protein molecules form a dodecamer with four trimers arranged in a tetrahedral manner. The classical lid adopts an open conformation although a sulfate ion is observed in the substrate binding site	Acinetobacter baumannii

Organism

Organism	UniProt	Comment	Textmining
Acinetobacter baumannii	A3M692	-	-
Acinetobacter baumannii ATCC 17978	A3M692	-	-

Subunits

Subunits	Comment	Organism
?	x * 16000, SDS-PAGE	Acinetobacter baumannii

Use of this online version of BRENDA is free under the CC BY 4.0 license. See terms of use for full details.

Release 2023.1 (January 2023)