CRYSTALLOGRAPHIC STRUCTURE OF A RELAXED GLUTAMINE SYNTHETASE FROM MYCOBACTERIUM TUBERCULOSIS
The structure was published by Gill, H.S., Pfluegl, G.M., and Eisenberg, D., in 2002 in a paper entitled "Multicopy crystallographic refinement of a relaxed glutamine synthetase from Mycobacterium tuberculosis highlights flexible loops in the enzymatic mechanism and its regulation." (abstract).
This crystal structure was determined using X-ray diffraction at a resolution of 2.4 Å and deposited in 2001.
The experimental data on which the structure is based was also deposited.
This PDB entry contains multiple copies of the structure of GLUTAMINE SYNTHETASE.
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 has more than one probable quaternary state observed. For more details see the quaternary structure page.
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: