3DM6
Beta-secretase 1 complexed with statine-based inhibitor
Summary for 3DM6
Entry DOI | 10.2210/pdb3dm6/pdb |
Descriptor | Beta-secretase 1, 5-[[(2S)-2-[[(3R,4S)-5-(3,5-difluorophenoxy)-3-hydroxy-4-[[3-(methyl-methylsulfonyl-amino)-5-[[(1R)-1-phenylethyl]carbamoyl]phenyl]carbonylamino]pentanoyl]amino]-3-methyl-butanoyl]amino]benzene-1,3-dicarboxylic acid, ISOPROPYL ALCOHOL, ... (4 entities in total) |
Functional Keywords | bace, beta-secretase, statine, inhibitor, alternative splicing, aspartyl protease, glycoprotein, hydrolase, membrane, protease, transmembrane, zymogen |
Biological source | Homo sapiens (Human) |
Cellular location | Membrane; Single-pass type I membrane protein: P56817 |
Total number of polymer chains | 3 |
Total formula weight | 139014.22 |
Authors | Lindberg, J.,Borkakoti, N.,Nystrom, S. (deposition date: 2008-06-30, release date: 2008-12-16, Last modification date: 2024-11-13) |
Primary citation | Back, M.,Nyhlen, J.,Kvarnstrom, I.,Appelgren, S.,Borkakoti, N.,Jansson, K.,Lindberg, J.,Nystrom, S.,Hallberg, A.,Rosenquist, S.,Samuelsson, B. Design, synthesis and SAR of potent statine-based BACE-1 inhibitors: exploration of P1 phenoxy and benzyloxy residues Bioorg.Med.Chem., 16:9471-9486, 2008 Cited by PubMed Abstract: Several BACE-1 inhibitors with low nanomolar level activities, encompassing a statine-based core structure with phenyloxymethyl- and benzyloxymethyl residues in the P1 position, are presented. The novel P1 modification introduced to allow the facile exploration of the S1 binding pocket of BACE-1, delivered highly promising inhibitors. PubMed: 18842420DOI: 10.1016/j.bmc.2008.09.041 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (2.6 Å) |
Structure validation
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