3HW1
Structure of Bace (beta secretase) in complex with ligand EV2
Summary for 3HW1
| Entry DOI | 10.2210/pdb3hw1/pdb |
| Related | 3HVG |
| Descriptor | Beta-secretase 1, 3-pyrrolidin-1-ylquinoxalin-2-amine, GLYCEROL, ... (4 entities in total) |
| Functional Keywords | protease, alzheimer's disease, aspartic protease, aspartyl protease, base, beta-secretase, glycoprotein, hydrolase, memapsin 2, amyloid precursor protein secretases, aspartic endopeptidases, fragment-based drug design, fluorescence polarisation, disulfide bond, 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 | 138118.01 |
| Authors | Godemann, R.,Madden, J.,Kramer, J.,Smith, M.A.,Barker, J.,Ebneth, A. (deposition date: 2009-06-17, release date: 2009-11-03, Last modification date: 2024-10-30) |
| Primary citation | Godemann, R.,Madden, J.,Kramer, J.,Smith, M.A.,Fritz, U.,Hesterkamp, T.,Barker, J.,Hoeppner, S.,Hallett, D.,Cesura, A.,Ebneth, A.,Kemp, J. Fragment-Based Discovery of BACE1 Inhibitors Using Functional Assays Biochemistry, 48:10743-10751, 2009 Cited by PubMed Abstract: Novel nonpeptidic inhibitors of beta-secretase (BACE1) have been discovered by employing a fragment-based biochemical screening approach. A diverse library of 20000 low-molecular weight compounds were screened and yielded 26 novel hits that were confirmed by biochemical and surface plasmon resonance secondary assays. We describe here fragment inhibitors cocrystallized with BACE1 in a flap open and flap closed conformation as determined by X-ray crystallography. PubMed: 19799414DOI: 10.1021/bi901061a PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.48 Å) |
Structure validation
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