Crystal structure of Thermus thermophilus glutamyl-tRNA synthetase complexed with ATP and Glu
The structure was published by Sekine, S., Nureki, O., Dubois, D.Y., et al., Lapointe, J., Vassylyev, D.G., and Yokoyama, S., in 2003 in a paper entitled "ATP binding by glutamyl-tRNA synthetase is switched to the productive mode by tRNA binding" (abstract).
This crystal structure was determined using X-ray diffraction at a resolution of 1.8 Å and deposited in 2002.
The experimental data on which the structure is based was also deposited.
The PDB entry contains the structure of Glutamyl-tRNA synthetase. This molecule has the UniProt identifier P27000 (SYE_THET8). The sample contained 468 residues which is 100% of the natural sequence. Out of 468 residues 468 were observed and are deposited in the PDB.
It also contains one or more heterogenic compounds (e.g., ligands, co-factors, ions, modified amino acids, etc.); see here for a complete list.
The molecule is most likely monomeric.
The following tables show cross-reference information to other databases (to obtain a list of all PDB entries sharing the same property or classification, click on the magnifying glass icon):
This entry contains 1 unique UniProt protein: