2BTY

Acetylglutamate kinase from Thermotoga maritima complexed with its inhibitor arginine

Replaces:  1UVV

Summary 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; PubMed: 16376937; DOI: 10.1016/J.JMB.2005.11.079

Experimental method

X-RAY DIFFRACTION (2.75 Å)