EC Number | Crystallization (Comment) | Organism |
---|---|---|
2.1.1.271 | - |
Priestia megaterium |
2.1.1.271 | 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 |
EC Number | Organism | UniProt | Comment | Textmining |
---|---|---|---|---|
2.1.1.271 | Priestia megaterium | - |
- |
- |
2.1.1.271 | Priestia megaterium | O87696 | - |
- |
EC Number | Purification (Comment) | Organism |
---|---|---|
2.1.1.271 | - |
Priestia megaterium |
EC Number | Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|---|
2.1.1.271 | S-adenosyl-L-methionine + cobalt-precorrin-4 | - |
Priestia megaterium | S-adenosyl-L-homocysteine + cobalt-precorrin-5 | - |
? |