BRENDA - Enzyme Database

A three-dimensional structure model of the complex of glutamyl-tRNA synthetase and its cognate tRNA

Tateno, M.; Nureki, O.; Sekine, S.i.; Kaneda, K.; Go, M.; Yokoyama, S.; FEBS Lett. 377, 77-81 (1995)

Data extracted from this reference:

Crystallization (Commentary)
EC Number
Crystallization
Organism
6.1.1.17
-
Thermus thermophilus
Metals/Ions
EC Number
Metals/Ions
Commentary
Organism
Structure
6.1.1.17
Zinc
-
Thermus thermophilus
Organism
EC Number
Organism
Primary Accession No. (UniProt)
Commentary
Textmining
6.1.1.17
Thermus thermophilus
-
wild-type and mutant enzymes
-
Substrates and Products (Substrate)
EC Number
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
6.1.1.17
ATP + L-glutamate + tRNAGlu
-
205
Thermus thermophilus
AMP + diphosphate + L-glutamyl-tRNAGlu
-
205
Thermus thermophilus
-
Crystallization (Commentary) (protein specific)
EC Number
Crystallization
Organism
6.1.1.17
-
Thermus thermophilus
Metals/Ions (protein specific)
EC Number
Metals/Ions
Commentary
Organism
Structure
6.1.1.17
Zinc
-
Thermus thermophilus
Substrates and Products (Substrate) (protein specific)
EC Number
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
6.1.1.17
ATP + L-glutamate + tRNAGlu
-
205
Thermus thermophilus
AMP + diphosphate + L-glutamyl-tRNAGlu
-
205
Thermus thermophilus
-