BACE-1 in complex with compound #34. Determined by X-ray diffraction at 1.47 Å resolution. Released 11 Dec 2019.
Explore 6UWV in 3D Show helices and sheets RCSB PDB PDBe
6UWV contains 27 α-helices and 56 β-strands across 2 chains. Residue ranges use author residue numbering, as in the PDB file, from PDBe. To see them in 3D, choose the Cartoon representation with Secondary structure coloring: helices, sheets and coils get different colors.
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 6-9 | 4 | 1 |
| β-strand | 13-20 | 8 | 1 |
| β-strand | 25-32 | 8 | 1 |
| β-strand | 38-41 | 4 | 1 |
| α-helix | 54-56 | 3 | |
| β-strand | 61-71 | 11 | 1 |
| β-strand | 74-86 | 13 | 1 |
| β-strand | 94-106 | 13 | 1 |
| β-strand | 117-120 | 4 | 1 |
| α-helix | 124-126 | 3 | |
| α-helix | 136-143 | 8 | |
| β-strand | 150-154 | 5 | 1 |
| α-helix | 163-168 | 6 | |
| β-strand | 172-176 | 5 | 1 |
| α-helix | 181-183 | 3 | |
| β-strand | 184-192 | 9 | 1 |
| β-strand | 196 | 1 | 2 |
| β-strand | 199 | 1 | 2 |
| β-strand | 200-201 | 2 | 3 |
| β-strand | 203-208 | 6 | 4 |
| β-strand | 211-212 | 2 | 4 |
| α-helix | 217-221 | 5 | |
| β-strand | 225-227 | 3 | 3 |
| β-strand | 234-237 | 4 | 3 |
| α-helix | 238-251 | 14 | |
| α-helix | 259-262 | 4 | |
| β-strand | 268-270 | 3 | 5 |
| α-helix | 277-279 | 3 | |
| α-helix | 281-282 | 2 | |
| β-strand | 283-288 | 6 | 4 |
| β-strand | 294-300 | 7 | 4 |
| α-helix | 302-305 | 4 | |
| β-strand | 306-309 | 4 | 5 |
| β-strand | 318-322 | 5 | 5 |
| β-strand | 324-327 | 4 | 3 |
| β-strand | 331-333 | 3 | 3 |
| α-helix | 335-338 | 4 | |
| β-strand | 341-346 | 6 | 1 |
| β-strand | 351-357 | 7 | 1 |
| β-strand | 369-375 | 7 | 4 |
| α-helix | 379-382 | 4 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 6-9 | 4 | 6 |
| β-strand | 13-20 | 8 | 6 |
| β-strand | 25-32 | 8 | 6 |
| β-strand | 38-41 | 4 | 6 |
| α-helix | 54-56 | 3 | |
| β-strand | 61-71 | 11 | 6 |
| β-strand | 74-86 | 13 | 6 |
| β-strand | 94-106 | 13 | 6 |
| β-strand | 117-120 | 4 | 6 |
| α-helix | 124-126 | 3 | |
| α-helix | 136-143 | 8 | |
| β-strand | 150-154 | 5 | 6 |
| α-helix | 163-168 | 6 | |
| β-strand | 172-176 | 5 | 6 |
| α-helix | 181-183 | 3 | |
| β-strand | 184-192 | 9 | 6 |
| β-strand | 196 | 1 | 7 |
| β-strand | 199 | 1 | 7 |
| β-strand | 200-201 | 2 | 8 |
| β-strand | 203-208 | 6 | 9 |
| β-strand | 211-212 | 2 | 9 |
| α-helix | 217-221 | 5 | |
| β-strand | 225-227 | 3 | 8 |
| β-strand | 234-237 | 4 | 8 |
| α-helix | 238-251 | 14 | |
| α-helix | 259-262 | 4 | |
| β-strand | 268-270 | 3 | 10 |
| α-helix | 277-279 | 3 | |
| α-helix | 281-282 | 2 | |
| β-strand | 283-288 | 6 | 9 |
| β-strand | 294-300 | 7 | 9 |
| α-helix | 302-305 | 4 | |
| β-strand | 306-309 | 4 | 10 |
| β-strand | 318-322 | 5 | 10 |
| β-strand | 324-327 | 4 | 8 |
| β-strand | 331-333 | 3 | 8 |
| α-helix | 335-338 | 4 | |
| β-strand | 341-346 | 6 | 6 |
| α-helix | 347-349 | 3 | |
| β-strand | 351-357 | 7 | 6 |
| β-strand | 369-375 | 7 | 9 |
| α-helix | 379-382 | 4 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Beta-secretase 1 | A, B | protein | 442 | Homo sapiens | P56817 (AlphaFold model) |
>6UWV_1 Beta-secretase 1 (chains A, B) MAGVLPAHGTQHGIRLPLRSGLGGAPLGLRLPRETDEEPEEPGRRGSFVEMVDNLRGKSG QGYYVEMTVGSPPQTLNILVDTGSSNFAVGAAPHPFLHRYYQRQLSSTYRDLRKGVYVPY TQGKWEGELGTDLVSIPHGPNVTVRANIAAITESDKFFINGSNWEGILGLAYAEIARPDD SLEPFFDSLVKQTHVPNLFSLQLCGAGFPLNQSEVLASVGGSMIIGGIDHSLYTGSLWYT PIRREWYYEVIIVRVEINGQDLKMDCKEYNYDKSIVDSGTTNLRLPKKVFEAAVKSIKAA SSTEKFPDGFWLGEQLVCWQAGTTPWNIFPVISLYLMGEVTNQSFRITILPQQYLRPVED VATSQDDCYKFAISQSSTGTVMGAVIMEGFYVVFDRARKRIGFAVSACHVHDEFRTAAVE GPFVTLDMEDCGYNIPQTDEST
| ID | Name | Formula | Copies |
|---|---|---|---|
| QK7 | (4aR,7aR)-7a-[(1R,2R)-2-(2-{[(1R,2R)-2-methylcyclopropyl]methoxy}propan-2-yl)cy… | C21 H31 N5 O S | 2 |
Water and common crystallization additives (GOL, SO4) are not listed.
Preparation and biological evaluation of BACE1 inhibitors: Leveraging trans-cyclopropyl moieties as ligand efficient conformational constraints. Winneroski, L.L., Erickson, J.A., Green, S.J. et al. Bioorg Med Chem (2020) 28:115194-115194. DOI 10.1016/j.bmc.2019.115194 · PubMed
Other PDB entries of the same protein (UniProt P56817 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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