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4NUA

The effects of Lysine 200 and Phenylalanine 239 Farnesyl Pyrophosphate Synthase (FPPS) mutations on the catalytic activity, crystal structure and inhibition by nitrogen containing bisphosphonates

Summary for 4NUA
Entry DOI10.2210/pdb4nua/pdb
Related1YQ7 4N9U 4NG6 4NKE 4NKF
DescriptorFarnesyl pyrophosphate synthase, 1-HYDROXY-2-(3-PYRIDINYL)ETHYLIDENE BIS-PHOSPHONIC ACID, MAGNESIUM ION, ... (6 entities in total)
Functional Keywordscholesterol synthesis, alpha-helical prenyltransferase fold, transferase, isoprene synthesis, lipid synthesis, steroid biosynthesis, isoprenoid pathway, dimethylallyl pyrophosphate, isopentenyl pyrophosphate
Biological sourceHomo sapiens (human)
Cellular locationCytoplasm: P14324
Total number of polymer chains1
Total formula weight43894.26
Authors
Tsoumpra, M.K.,Barnett, B.L.,Muniz, J.R.C.,Walter, R.L.,Ebetino, F.H.,von Delft, F.,Russell, R.G.G.,Oppermann, U.,Dunford, J.E. (deposition date: 2013-12-03, release date: 2014-11-19, Last modification date: 2023-09-20)
Primary citationTsoumpra, M.K.,Barnett, B.L.,Muniz, J.R.C.,Walter, R.L.,Ebetino, F.H.,von Delft, F.,Russell, R.G.G.,Oppermann, U.,Dunford, J.E.
The effects of Lysine 200 and Phenylalanine 239 Farnesyl Pyrophosphate Synthase (FPPS) mutations on the catalytic activity, crystal structure and inhibition by nitrogen containing bisphosphonates
To be Published,
Experimental method
X-RAY DIFFRACTION (1.43 Å)
Structure validation

222926

数据于2024-07-24公开中

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