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Literature summary for 3.1.2.20 extracted from
- Crystal structure of a putative acyl-CoA thioesterase from Xanthomonas campestris (XC229) adopts a tetrameric hotdog fold of egamma mode (2006), Proteins Struct. Funct. Bioinform., 64, 823-826.
Crystallization (Commentary)
| Crystallization (Comment) | Organism |
|---|---|
| hanging-drop vapor diffusion method at 20°C, 1.8 A resolution, the crystal structure adopts a unique tetramer of epsilongamma mode with extensive subunit H-bonding/salt bridge interactions | Xanthomonas campestris |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Xanthomonas campestris | - |
- |
- |
| Xanthomonas campestris XC229 | - |
- |
- |
Synonyms
| Synonyms | Comment | Organism |
|---|---|---|
| acyl-CoA thioesterase | - |
Xanthomonas campestris |
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Release 2023.1 (January 2023)
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