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EC Number	Crystallization (Commentary)
2.1.1.196	homotetrameric apo form of CbiT crystallized in several space groups, to about 2.5 A resolution, and in complex with S-adenosyl-L-homocysteine, to 1.9 A resolution. The protein shows structural similarity to Rossmann-like S-adenosyl-methionine-dependent methyltransferases, and the cocrystal structure shows that it binds S-adenosyl-methionine in standard geometry near a binding pocket that can accommodate a precorrin substrate. CbiT probably functions as a precorrin methyltransferase

EC Number

Crystallization (Commentary)

2.1.1.196

homotetrameric apo form of CbiT crystallized in several space groups, to about 2.5 A resolution, and in complex with S-adenosyl-L-homocysteine, to 1.9 A resolution. The protein shows structural similarity to Rossmann-like S-adenosyl-methionine-dependent methyltransferases, and the cocrystal structure shows that it binds S-adenosyl-methionine in standard geometry near a binding pocket that can accommodate a precorrin substrate. CbiT probably functions as a precorrin methyltransferase

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Release 2023.1 (January 2023)