Crystal structure of E. coli Threonyl-tRNA synthetase bound to a novel inhibitor
The structure was published by Teng, M., Hilgers, M.T., Cunningham, M.L., et al., Hough, G.W., Shaw, K.J., and Finn, J., in 2013 in a paper entitled "Identification of bacteria-selective threonyl-tRNA synthetase substrate inhibitors by structure-based design." (abstract).
This crystal structure was determined using X-ray diffraction at a resolution of 1.9 Å and deposited in 2012.
The experimental data on which the structure is based was also deposited.
This PDB entry contains multiple copies of the structure of Threonine--tRNA ligase.
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 most likely forms homodimers.
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: