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Literature summary for 2.7.1.100 extracted from
- ADP-2Ho as a phasing tool for nucleotide-containing proteins (2007), Acta Crystallogr. Sect. D, 63, 493-499.
Cloned(Commentary)
| Cloned (Comment) | Organism |
|---|---|
- |
Bacillus subtilis |
Crystallization (Commentary)
| Crystallization (Comment) | Organism |
|---|---|
| ADP-2Ho and ADP-2Mg complexes | Bacillus subtilis |
Metals/Ions
| Metals/Ions | Comment | Organism | Structure |
|---|---|---|---|
| Ho3+ | trivalent holmium ions can isomorphously replace Mg2+ form an ADP-2Ho complex in the nucleotide-binding domain of Bacillus subtilis 5-methylthioribose kinase The structure of ADP-2Ho reveals that the two Ho ions are approximately 4 A apart and are likely to share their ligands: the phosphoryl O atoms of ADP and a water molecule | Bacillus subtilis |  |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Bacillus subtilis | O31663 | - |
- |
Purification (Commentary)
| Purification (Comment) | Organism |
|---|---|
- |
Bacillus subtilis |
Synonyms
| Synonyms | Comment | Organism |
|---|---|---|
| 5-methylthioribose kinase | - |
Bacillus subtilis |
| MTR kinase | - |
Bacillus subtilis |
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