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Literature summary for 6.1.1.18 extracted from
- Structural basis of anticodon loop recognition by glutaminyl-tRNA synthetase (1991), Nature, 352, 213-218.
Crystallization (Commentary)
| Crystallization (Comment) | Organism |
|---|---|
| 2.5 A resolution | Escherichia coli |
| structure of the enzyme with its cognate glutaminyl-tRNA and ATP | Escherichia coli |
| the entire anticodon loop provides essential sites for glutaminyl tRNA synthetase discrimination among tRNA molecules | Escherichia coli |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Escherichia coli | - |
- |
- |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| ATP + L-glutamine + tRNAGln | - |
Escherichia coli | AMP + diphosphate + L-glutaminyl-tRNAGln | - |
? |  |
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Release 2023.1 (January 2023)
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