ACETYLGLUTAMATE KINASE FROM ESCHERICHIA COLI COMPLEXED WITH MGADP, N-ACETYL-L-GLUTAMATE AND THE TRANSITION-STATE MIMIC ALF4-
The structure was published by Gil-Ortiz, F., Ramon-Maiques, S., Fita, I., and Rubio, V., in 2003 in a paper entitled "The Course of Phosphorus in the Reaction of N-Acetyl-L-Glutamate Kinase, Determined from the Structures of Crystalline Complexes, Including a Complex with an Alf(4)(-) Transition State Mimic" (abstract).
This crystal structure was determined using X-ray diffraction at a resolution of 1.91 Å and deposited in 2003.
The experimental data on which the structure is based was also deposited.
The PDB entry contains the structure of ACETYLGLUTAMATE KINASE. This molecule has the UniProt identifier P0A6C8 (ARGB_ECOLI). The sample contained 258 residues which is 100% of the natural sequence. Out of 258 residues 258 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 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: