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4N9U

The role of lysine 200 in the human farnesyl pyrophosphate synthase catalytic mechanism and the mode of inhibition by the nitrogen-containing bisphosphonates

Summary for 4N9U
Entry DOI10.2210/pdb4n9u/pdb
Related1YQ7 4KFA 4KPD 4KPJ 4KQ5 4KQS 4KQU 4NG6 4NKE 4NKF 4NUA
DescriptorFarnesyl pyrophosphate synthase, MAGNESIUM ION, 1-HYDROXY-2-(3-PYRIDINYL)ETHYLIDENE BIS-PHOSPHONIC ACID, ... (5 entities in total)
Functional Keywordsalpha-helical prenyltransferase fold, isoprene biosynthesis, lipid synthesis, steroid biosynthesis, dimethylallyl pyrophosphate, isopentenyl pyrophosphate, transferase
Biological sourceHomo sapiens (human)
Cellular locationCytoplasm: P14324
Total number of polymer chains1
Total formula weight43583.04
Authors
Tsoumpra, M.K.,Muniz, J.R.C.,Barnett, B.L.,Pilka, E.,Kwaasi, A.A.,Kavanagh, K.L.,Evdokimov, A.,Walter, R.L.,Ebetino, F.H.,Oppermann, U.,Russell, R.G.G.,Dunford, J.E. (deposition date: 2013-10-21, release date: 2014-10-22, Last modification date: 2023-09-20)
Primary citationTsoumpra, M.K.,Muniz, J.R.C.,Barnett, B.L.,Pilka, E.,Kwaasi, A.A.,Kavanagh, K.L.,Evdokimov, A.,Walter, R.L.,Ebetino, F.H.,Oppermann, U.,Russell, R.G.G.,Dunford, J.E.
The role of lysine 200 in the human farnesyl pyrophosphate synthase catalytic mechanism and the mode of inhibition by the nitrogen-containing bisphosphonates
TO BE PUBLISHED,
Experimental method
X-RAY DIFFRACTION (2.11 Å)
Structure validation

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