EC Number | Crystallization (Comment) | Organism |
---|---|---|
3.6.5.3 | structure of the mutant enzyme T84A in complex with the non-hydrolysable GTP analogue GDPNP | Thermus thermophilus |
EC Number | Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|---|
3.6.5.3 | GTP + H2O | Thermus thermophilus | elongation factor G catalyzes the translocation step in protein synthesis on the ribosome | GDP + phosphate | - |
? |
EC Number | Organism | UniProt | Comment | Textmining |
---|---|---|---|---|
3.6.5.3 | Thermus thermophilus | - |
- |
- |
EC Number | Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|---|
3.6.5.3 | GTP + H2O | elongation factor G catalyzes the translocation step in protein synthesis on the ribosome | Thermus thermophilus | GDP + phosphate | - |
? | |
3.6.5.3 | GTP + H2O | enzyme-GTP and enzyme-GDP conformations in solution are very similar. The major contribution to the active GTPase conformation, which is quite different, therefore comes from its interaction with the ribosome | Thermus thermophilus | GDP + phosphate | - |
? |
EC Number | Synonyms | Comment | Organism |
---|---|---|---|
3.6.5.3 | EF-G | - |
Thermus thermophilus |
3.6.5.3 | elongation factor G | - |
Thermus thermophilus |