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Literature summary extracted from
- The crystal structure of the lysyl-tRNA synthetase from Escherichia coli (1995), Structure, 15, 163-176.
Crystallization (Commentary)
| EC Number | Crystallization (Comment) | Organism |
|---|---|---|
| 6.1.1.6 | determined to 2.8 A resolution with lysine bound to the active site | Escherichia coli |
Organism
| EC Number | Organism | UniProt | Comment | Textmining |
|---|---|---|---|---|
| 6.1.1.6 | Escherichia coli | - |
- |
- |
Substrates and Products (Substrate)
| EC Number | Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|---|
| 6.1.1.6 | ATP + lysine + tRNALys | - |
Escherichia coli | AMP + L-lysyl-tRNALys + diphosphate | - |
? |  |
Subunits
| EC Number | Subunits | Comment | Organism |
|---|---|---|---|
| 6.1.1.6 | dimer | homodimer | Escherichia coli |
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