6N7Y

Crystal structure of human FPPS in complex with an allosteric inhibitor MIT-01-102

Summary for 6N7Y

Entry DOI	10.2210/pdb6n7y/pdb
Descriptor	Farnesyl pyrophosphate synthase, GLYCEROL, [(1R)-1-{[6-(4-methylphenyl)thieno[2,3-d]pyrimidin-4-yl]amino}-2-phenylethyl]phosphonic acid, ... (5 entities in total)
Functional Keywords	transferase, transferase-transferase inhibitor complex, transferase/transferase inhibitor
Biological source	Homo sapiens (Human)
Total number of polymer chains	1
Total formula weight	43757.49
Authors	Park, J.,Berghuis, A.M. (deposition date: 2018-11-28, release date: 2019-11-06, Last modification date: 2023-10-11)
Primary citation	Feng, Y.,Park, J.,Li, S.G.,Boutin, R.,Viereck, P.,Schilling, M.A.,Berghuis, A.M.,Tsantrizos, Y.S. Chirality-Driven Mode of Binding of alpha-Aminophosphonic Acid-Based Allosteric Inhibitors of the Human Farnesyl Pyrophosphate Synthase (hFPPS). J.Med.Chem., 62:9691-9702, 2019 Cited by PubMed Abstract: Thienopyrimidine-based allosteric inhibitors of the human farnesyl pyrophosphate synthase (hFPPS), characterized by a chiral α-aminophosphonic acid moiety, were synthesized as enantiomerically enriched pairs, and their binding mode was investigated by X-ray crystallography. A general consensus in the binding orientation of all ()- and ()-enantiomers was revealed. This finding is a prerequisite for establishing a reliable structure-activity relationship (SAR) model. PubMed: 31577901 DOI: 10.1021/acs.jmedchem.9b01104 PDB entries with the same primary citation
Experimental method	X-RAY DIFFRACTION (2 Å)

Structure validation