1CM2
STRUCTURE OF HIS15ASP HPR AFTER HYDROLYSIS OF RINGED SPECIES.
Summary for 1CM2
| Entry DOI | 10.2210/pdb1cm2/pdb |
| Related | 1CM3 |
| Descriptor | HISTIDINE-CONTAINING PROTEIN (2 entities in total) |
| Functional Keywords | phosphotransferase, succinimide, isoimide, transferase |
| Biological source | Escherichia coli |
| Cellular location | Cytoplasm: P0AA04 |
| Total number of polymer chains | 1 |
| Total formula weight | 9106.27 |
| Authors | Napper, S.,Delbaere, L.T.J.,Waygood, E.B. (deposition date: 1999-05-13, release date: 2000-05-17, Last modification date: 2024-04-03) |
| Primary citation | Napper, S.,Delbaere, L.T.,Waygood, E.B. The aspartyl replacement of the active site histidine in histidine-containing protein, HPr, of the Escherichia coli Phosphoenolpyruvate:Sugar phosphotransferase system can accept and donate a phosphoryl group. Spontaneous dephosphorylation of acyl-phosphate autocatalyzes an internal cyclization J.Biol.Chem., 274:21776-21782, 1999 Cited by PubMed: 10419492DOI: 10.1074/jbc.274.31.21776 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.8 Å) |
Structure validation
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