Literature summary for 2.4.1.306 extracted from

Li, F.; Li, S.; Liu, X.; Yang, X.; Wang, P.; Shen, Y.
The structure of WbnH in a near active state (2015), Protein Cell, 6, 615-618.

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Crystallization (Commentary)

Crystallization (Comment)	Organism
to 2.2 A resolution, and modeling of both the donor substrate UDP-GalNAC and the acceptor substrate analog 1-L-Ins-1-P into the structure. UDP-GalNAC primarily binds to the C-lobe (i.e. residues 167322) and is surrounded by four conserved residues (i.e., His109, Lys192, Glu256 and Glu264). The acceptor analog 1-L-Ins-1-P binds to the N-lobe, and the tail portion extends into the solvent region in the model	Escherichia coli

Crystallization (Comment)

Organism

to 2.2 A resolution, and modeling of both the donor substrate UDP-GalNAC and the acceptor substrate analog 1-L-Ins-1-P into the structure. UDP-GalNAC primarily binds to the C-lobe (i.e. residues 167322) and is surrounded by four conserved residues (i.e., His109, Lys192, Glu256 and Glu264). The acceptor analog 1-L-Ins-1-P binds to the N-lobe, and the tail portion extends into the solvent region in the model

Escherichia coli

Organism

Organism	UniProt	Comment	Textmining
Escherichia coli	-	-	-
Escherichia coli O86:H2	-	-	-

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Release 2023.1 (January 2023)