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Literature summary 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 .
    View publication on PubMed

Cloned(Commentary)

EC Number Cloned (Comment) Organism
4.2.1.10 expression in Escherichia coli Acinetobacter baumannii

Crystallization (Commentary)

EC Number Crystallization (Comment) Organism
4.2.1.10 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

EC Number Organism UniProt Comment Textmining
4.2.1.10 Acinetobacter baumannii A3M692
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4.2.1.10 Acinetobacter baumannii ATCC 17978 A3M692
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Subunits

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