3A29

Crystal structure of human liver FBPase in complex with tricyclic inhibitor

Summary for 3A29

Entry DOI	10.2210/pdb3a29/pdb
Descriptor	Fructose-1,6-bisphosphatase 1, 2-amino-4,5-dihydronaphtho[1,2-d][1,3]thiazol-8-yl dihydrogen phosphate (3 entities in total)
Functional Keywords	hydrolase, allosteric enzyme, carbohydrate metabolism, disease mutation, gluconeogenesis, magnesium, metal-binding, polymorphism
Biological source	Homo sapiens (human)
Total number of polymer chains	4
Total formula weight	148105.93
Authors	Takahashi, M.,Sone, J.,Hanzawa, H. (deposition date: 2009-05-08, release date: 2009-10-06, Last modification date: 2023-11-01)
Primary citation	Tsukada, T.,Takahashi, M.,Takemoto, T.,Kanno, O.,Yamane, T.,Kawamura, S.,Nishi, T. Synthesis, SAR, and X-ray structure of tricyclic compounds as potent FBPase inhibitors Bioorg.Med.Chem.Lett., 19:5909-5912, 2009 Cited by PubMed Abstract: With the aim of discovering a novel class of fructose-1,6-bisphosphatase (FBPase) inhibitors, a series of compounds based on tricyclic scaffolds was synthesized. Extensive SAR studies led to the finding of 8l with an IC50 value of 0.013 microM against human FBPase. An X-ray crystallographic study revealed that 8l bound at AMP binding sites of human liver FBPase with hydrogen bonding interactions similar to AMP. PubMed: 19762234 DOI: 10.1016/j.bmcl.2009.08.081 PDB entries with the same primary citation
Experimental method	X-RAY DIFFRACTION (2.6 Å)

Structure validation