Literature summary for 2.1.1.13 extracted from

Bandarian, V.; Pattridge, K.A.; Lennon, B.W.; Huddler, D.P.; Matthews, R.G.; Ludwig, M.L.
Domain alteration switches B12-dependent methionine synthase to the activation conformation (2002), Nat. Struct. Biol., 9, 53-56.

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Activating Compound

Activating Compound	Comment	Organism	Structure
S-adenosyl-L-methionine	required	Escherichia coli

Crystallization (Commentary)

Crystallization (Comment)	Organism
3.0 A structure of a 65000 Da C-terminal fragment of methionine synthase that spans the cobalamin- and the S-adenosylmethionine-binding domains, arranged in a conformation suitable for the methyl transfer from S-adenosylmethionine to cobalamin that occurs during activation	Escherichia coli

Organism

Organism	UniProt	Comment	Textmining
Escherichia coli	P13009	-	-

Cofactor

Cofactor	Comment	Organism	Structure
vitamin B12	dependent	Escherichia coli

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Release 2023.1 (January 2023)