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Literature summary for 1.4.1.4 extracted from
- Structural and thermodynamic studies on a salt-bridge triad in the NADP-binding domain of glutamate dehydrogenase from Thermotoga maritima: cooperativity and electrostatic contribution to stability (2002), Biochemistry, 41, 15524-15535.
Crystallization (Commentary)
| Crystallization (Comment) | Organism |
|---|---|
| cofactor binding domain of glutamate dehydrogenase, sitting-drop vapor diffusion method. X-ray structure of the domain of wild-type enzyme and mutant enzyme R190A/E231A/K193A is solved at 1.43 A | Thermotoga maritima |
Protein Variants
| Protein Variants | Comment | Organism |
|---|---|---|
| R190A/E231A/K193A | mutation has no effect on the overall conformation of the protein | Thermotoga maritima |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Thermotoga maritima | - |
- |
- |
Cofactor
| Cofactor | Comment | Organism | Structure |
|---|---|---|---|
| NADP+ | - |
Thermotoga maritima |  |
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Release 2023.1 (January 2023)
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