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EC Number	Crystallization (Commentary)
4.2.3.24	3D-modeling of structure. Predicted model shows that the putative ADS3963 protein contains 72% of alpha-helices, 23% beta-turns and 26% of random coils. Based on docking studies with substrate farnesyl diphosphate, the stretches Ala321-Ala324-Lys-398, Ala234-Val237-Phe283-Thr286-Tyr-287, Ser94-Met95-Trp141-Trp430-Asn434, Ser94-Arg96-Glu104-Leu107-Lys142-Lys431, Lys137-Arg143-Ile147-Ala150-Gln151-Leu478 and Ser218-Gly219-Tyr224-Arg228-Cys352-Met356-Aln450 may constitute to substrate binding

EC Number

Crystallization (Commentary)

4.2.3.24

3D-modeling of structure. Predicted model shows that the putative ADS3963 protein contains 72% of alpha-helices, 23% beta-turns and 26% of random coils. Based on docking studies with substrate farnesyl diphosphate, the stretches Ala321-Ala324-Lys-398, Ala234-Val237-Phe283-Thr286-Tyr-287, Ser94-Met95-Trp141-Trp430-Asn434, Ser94-Arg96-Glu104-Leu107-Lys142-Lys431, Lys137-Arg143-Ile147-Ala150-Gln151-Leu478 and Ser218-Gly219-Tyr224-Arg228-Cys352-Met356-Aln450 may constitute to substrate binding

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Release 2023.1 (January 2023)