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EBI PDBe PDBeView

PDBe Entry: 2f89 view

Crystal structure of human FPPS in complex with pamidronate
Summary
Header TRANSFERASEsearch
Method X-RAY DIFFRACTION
Experiment Resolution: 2.6 Å, R-factor: 20.6%, Free R-factor: 26.7%, Spacegroup: P 41 21 2
Released 28/02/2006, deposition: 02/12/2005, last revision: 24/02/2009
Authors Rondeau, J.-M.search; Bitsch, F.search; Bourgier, E.search; Geiser, M.search; Hemmig, R.search; Kroemer, M.search; Lehmann, S.search; Ramage, P.search; Rieffel, S.search; Strauss, A.search; Green, J.R.search; Jahnke, W.search
Primary citation Structural basis for the exceptional in vivo efficacy of bisphosphonate drugs.
CHEMMEDCHEMsearch vol:1, pag:267-273 (2006) [PubMed ID 16892359 ]search
Keywords MEVALONATE PATHWAY; ISOPRENE BIOSYNTHESIS; CHOLESTEROL BIOSYNTHESIS; BISPHOSPHONATE INHIBITORsearch, TRANSFERASEsearch
EC 2.5.1.1 ExPASy BRENDA search 2.5.1.10 ExPASy BRENDA search (F)
Organism Homo sapiens(human) 9606search(F)
UniProt Farnesyl pyrophosphate synthetase (FPP synthetase) (FPS) (Farnesyl diphosphate synthetase) [Includes: Dimethylallyltranstransferase (EC 2.5.1.1); Geranyltranstransferase (EC 2.5.1.10)] P14324search (F)
Solvent F
Related entries 2f7m, 2f8c, 2f8z, 2f92, 2f94, 2f9k
Polymers
Id Name Type UniProt Residues Observed
F Farnesyl Diphosphate Synthase Protein P14324 (FPPS_HUMAN)search
 350 98%
Heterogens
Id Name Ligands
F PHOSPHATE ION PO4 search
F MANGANESE (II) ION MN search
F PAMIDRONATE 210 search
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