2.1.1.271: cobalt-precorrin-4 methyltransferase

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For detailed information about cobalt-precorrin-4 methyltransferase, go to the full flat file.

Reaction

Synonyms

CbiF, Cobalt-precorrin-4 C(11)-methyltransferase, cobalt-precorrin-4 transmethylase

ECTree

2 Transferases

2.1 Transferring one-carbon groups

2.1.1 Methyltransferases

2.1.1.271 cobalt-precorrin-4 methyltransferase

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Results	in table
1135	AA Sequence
3	Cloned(Commentary)
2	Cofactor
4	Crystallization (Commentary)
3	General Information
1	General Stability
3	Molecular Weight [Da]
6	Natural Substrates/ Products (Substrates)
11	Organism
5	Pathway
2	Protein Variants
3	Purification (Commentary)
2	Reaction
7	Reference
2	Storage Stability
13	Substrates and Products (Substrate)
2	Subunits
7	Synonyms
1	Systematic Name

Crystallization

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Crystallization on EC 2.1.1.271 - cobalt-precorrin-4 methyltransferase

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2 entries

to 2.4 A resolution. Protein shows two discrete crystal forms, and crystals only grow in the presence of either S-adenosyl-L-methionine or S-adenosyl-L-homocysteine

Priestia megaterium

O87696

35080

to 2.4 A resolution. The enzyme contains two alpha/beta domains forming a trough in which S-adenosyl-L-homocysteine binds. The entire structure follows a beta-alpha repeating pattern with the single exception of a beta-hairpin late in the C-terminal domain. A second crystal form determined at 3.1 A resolution highlights the flexibility of two loops around the S-adenosyl-L-homocysteine-binding site

Priestia megaterium

O87696

35081