Literature summary extracted from

Lebbink, J.H.; Consalvi, V.; Chiaraluce, R.; Berndt, K.D.; Ladenstein, R.
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)

EC Number	Crystallization (Comment)	Organism
1.4.1.4	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

EC Number	Protein Variants	Comment	Organism
1.4.1.4	R190A/E231A/K193A	mutation has no effect on the overall conformation of the protein	Thermotoga maritima

Organism

EC Number	Organism	UniProt	Comment	Textmining
1.4.1.4	Thermotoga maritima	-	-	-

Cofactor

EC Number	Cofactor	Comment	Organism	Structure
1.4.1.4	NADP+	-	Thermotoga maritima

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Release 2023.1 (January 2023)