Literature summary for 3.2.1.39 extracted from

Hong, T.Y.; Hsiao, Y.Y.; Meng, M.; Li, T.T.
The 1.5 A structure of endo-1,3-beta-glucanase from Streptomyces sioyaensis: evolution of the active-site structure for 1,3-beta-glucan-binding specificity and hydrolysis (2008), Acta Crystallogr. Sect. D, 64, 964-970.

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Cloned(Commentary)

Cloned (Comment)	Organism
expression in Escherichia coli	Streptomyces sioyaensis

Crystallization (Commentary)

Crystallization (Comment)	Organism
catalytic domain, to 1.5 A resolution. The overall structure contains two antiparallel six- and seven-stranded beta-sheets stacked in a beta-sandwich jelly-roll motif. The active-site cleft of the enzyme shows the closure of one end primarily caused by two protruding loop insertions and two key residues, Y38 and Y134	Streptomyces sioyaensis

Organism

Organism	UniProt	Comment	Textmining
Streptomyces sioyaensis	Q9L816	-	-

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Release 2023.1 (January 2023)