5JA0
Crystal structure of human FPPS with allosterically bound FPP
Summary for 5JA0
Entry DOI | 10.2210/pdb5ja0/pdb |
Descriptor | Farnesyl pyrophosphate synthase, PHOSPHATE ION, FARNESYL DIPHOSPHATE, ... (4 entities in total) |
Functional Keywords | transferase |
Biological source | Homo sapiens (Human) |
Cellular location | Cytoplasm: P14324 |
Total number of polymer chains | 1 |
Total formula weight | 43622.28 |
Authors | Park, J.,Zielinski, M.,Tsantrizos, Y.S.,Berghuis, A.M. (deposition date: 2016-04-11, release date: 2017-01-25, Last modification date: 2023-09-27) |
Primary citation | Park, J.,Zielinski, M.,Magder, A.,Tsantrizos, Y.S.,Berghuis, A.M. Human farnesyl pyrophosphate synthase is allosterically inhibited by its own product. Nat Commun, 8:14132-14132, 2017 Cited by PubMed: 28098152DOI: 10.1038/ncomms14132 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (1.9 Å) |
Structure validation
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