1GPM
ESCHERICHIA COLI GMP SYNTHETASE COMPLEXED WITH AMP AND PYROPHOSPHATE
Summary for 1GPM
| Entry DOI | 10.2210/pdb1gpm/pdb |
| Descriptor | GMP SYNTHETASE, PHOSPHATE ION, PYROPHOSPHATE 2-, ... (7 entities in total) |
| Functional Keywords | class i glutamine amidotransferase, n-type atp pyrophosphatase, transferase (glutamine amidotransferase) |
| Biological source | Escherichia coli |
| Total number of polymer chains | 4 |
| Total formula weight | 238314.19 |
| Authors | Tesmer, J.J.G. (deposition date: 1995-04-04, release date: 1996-01-29, Last modification date: 2024-02-07) |
| Primary citation | Tesmer, J.J.,Klem, T.J.,Deras, M.L.,Davisson, V.J.,Smith, J.L. The crystal structure of GMP synthetase reveals a novel catalytic triad and is a structural paradigm for two enzyme families. Nat.Struct.Biol., 3:74-86, 1996 Cited by PubMed Abstract: The crystal structure of GMP synthetase serves as a prototype for two families of metabolic enzymes. The Class I glutamine amidotransferase domain of GMP synthetase is found in related enzymes of the purine, pyrimidine, tryptophan, arginine, histidine and folic acid biosynthetic pathways. This domain includes a conserved Cys-His-Glu triad and is representative of a new family of enzymes that use a catalytic triad for enzymatic hydrolysis. The structure and conserved sequence fingerprint of the nucleotide-binding site in a second domain of GMP synthetase are common to a family of ATP pyrophosphatases, including NAD synthetase, asparagine synthetase and argininosuccinate synthetase. PubMed: 8548458DOI: 10.1038/nsb0196-74 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.2 Å) |
Structure validation
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