1GS5
N-acetyl-L-glutamate kinase from Escherichia coli complexed with its substrate N-acetylglutamate and its substrate analog AMPPNP
Summary for 1GS5
Entry DOI | 10.2210/pdb1gs5/pdb |
Descriptor | ACETYLGLUTAMATE KINASE, N-ACETYL-L-GLUTAMATE, PHOSPHOAMINOPHOSPHONIC ACID-ADENYLATE ESTER, ... (5 entities in total) |
Functional Keywords | carbamate kinase, amino acid kinase, arginine biosynthesis, phosphoryl group transfer, transferase |
Biological source | ESCHERICHIA COLI |
Cellular location | Cytoplasm (Probable): P11445 |
Total number of polymer chains | 1 |
Total formula weight | 27906.16 |
Authors | Ramon-Maiques, S.,Marina, A.,Gil-Ortiz, F.,Fita, I.,Rubio, V. (deposition date: 2001-12-28, release date: 2002-05-16, Last modification date: 2023-12-13) |
Primary citation | Ramon-Maiques, S.,Marina, A.,Gil-Ortiz, F.,Fita, I.,Rubio, V. Structure of Acetylglutamate Kinase, a Key Enzyme for Arginine Biosynthesis and a Prototype for the Amino Acid Kinase Enzyme Family, During Catalysis Structure, 10:329-, 2002 Cited by PubMed: 12005432DOI: 10.1016/S0969-2126(02)00721-9 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (1.5 Å) |
Structure validation
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