6YP4
Putative adenylyl cyclase HpAC1 from Hippeastrum reveals a dominant triphophatase activity
Summary for 6YP4
Entry DOI | 10.2210/pdb6yp4/pdb |
Descriptor | Adenylate cyclase, PHOSPHOMETHYLPHOSPHONIC ACID GUANYLATE ESTER, MAGNESIUM ION, ... (6 entities in total) |
Functional Keywords | triphosphatase, plant, pppase, gtp analog, substrate complex, substrate specificity, hydrolase |
Biological source | Hippeastrum hybrid cultivar |
Total number of polymer chains | 1 |
Total formula weight | 24968.62 |
Authors | Kleinboelting, S.,Steegborn, C. (deposition date: 2020-04-15, release date: 2020-11-04, Last modification date: 2024-01-24) |
Primary citation | Kleinboelting, S.,Miehling, J.,Steegborn, C. Crystal structure and enzymatic characterization of the putative adenylyl cyclase HpAC1 from Hippeastrum reveal dominant triphosphatase activity. J.Struct.Biol., 212:107649-107649, 2020 Cited by PubMed: 33075486DOI: 10.1016/j.jsb.2020.107649 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (1.94541097376 Å) |
Structure validation
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