3DDF

GOLGI MANNOSIDASE II complex with (3R,4R,5R)-3,4-Dihydroxy-5-({[(1R)-2-hydroxy-1 phenylethyl]amino}methyl) pyrrolidin-2-one

Summary for 3DDF

Entry DOI	10.2210/pdb3ddf/pdb
Related	1HTY 1QWN 2ALW 2F18 2F1A 2F1B 2F7O 2F7P 3BLB 3BUB 3DDG
Descriptor	alpha-mannosidase 2, 2-acetamido-2-deoxy-beta-D-glucopyranose, ZINC ION, ... (7 entities in total)
Functional Keywords	gh38 glycosidase, hydrolase
Biological source	Drosophila melanogaster (fruit fly)
Total number of polymer chains	1
Total formula weight	120490.88
Authors	Kuntz, D.A.,Rose, D.R.,Hoffman, D. (deposition date: 2008-06-05, release date: 2008-07-01, Last modification date: 2023-08-30)
Primary citation	Fiaux, H.,Kuntz, D.A.,Hoffman, D.,Janzer, R.C.,Gerber-Lemaire, S.,Rose, D.R.,Juillerat-Jeanneret, L. Functionalized pyrrolidine inhibitors of human type II alpha-mannosidases as anti-cancer agents: optimizing the fit to the active site Bioorg.Med.Chem., 16:7337-7346, 2008 Cited by PubMed Abstract: Refining the chemical structure of functionalized pyrrolidine-based inhibitors of Golgi alpha-mannosidase II (GMII) to optimize binding affinity provided a lead molecule that demonstrated nanomolar competitive inhibition of alpha-mannosidases II and an optimal fit in the active site of Drosophila GMII by X-ray crystallography. Esters of this lead compound also inhibited the growth of human glioblastoma and brain-derived endothelial cells more than the growth of non-tumoral human fibroblasts, suggesting their potential for anti-cancer therapy. PubMed: 18599296 DOI: 10.1016/j.bmc.2008.06.021 PDB entries with the same primary citation
Experimental method	X-RAY DIFFRACTION (1.2 Å)

Structure validation