2BTY
Acetylglutamate kinase from Thermotoga maritima complexed with its inhibitor arginine
Replaces: 1UVVSummary for 2BTY
Entry DOI | 10.2210/pdb2bty/pdb |
Descriptor | ACETYLGLUTAMATE KINASE, ARGININE, N-ACETYL-L-GLUTAMATE, ... (5 entities in total) |
Functional Keywords | n-acetyl-l-glutamate kinase, amino acid kinase, phosphoryl group transfer, arginine metabolism, transferase, arginine biosynthesis, amino-acid biosynthesis, kinase |
Biological source | THERMOTOGA MARITIMA |
Cellular location | Cytoplasm (By similarity): Q9X2A4 |
Total number of polymer chains | 3 |
Total formula weight | 92289.09 |
Authors | Gil-Ortiz, F.,Fernandez-Murga, M.L.,Fita, I.,Rubio, V. (deposition date: 2005-06-08, release date: 2005-12-13, Last modification date: 2023-12-13) |
Primary citation | Ramon-Maiques, S.,Fernandez-Murga, M.L.,Gil-Ortiz, F.,Vagin, A.,Fita, I.,Rubio, V. Structural Bases of Feed-Back Control of Arginine Biosynthesis, Revealed by the Structure of Two Hexameric N-Acetylglutamate Kinases, from Thermotoga Maritima and Pseudomonas Aeruginosa J.Mol.Biol., 356:695-, 2006 Cited by PubMed: 16376937DOI: 10.1016/J.JMB.2005.11.079 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (2.75 Å) |
Structure validation
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