Cyrstal structure of human alpha-synuclein (10-42) fused to maltose binding protein (MBP). Determined by X-ray diffraction at 1.54 Å resolution. Released 1 Jun 2011.
Explore 3Q26 in 3D Show helices and sheets RCSB PDB PDBe
3Q26 contains 28 α-helices and 24 β-strands across 1 chain. 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 |
|---|---|---|---|
| α-helix | 3-4 | 2 | |
| β-strand | 7-11 | 5 | 1 |
| α-helix | 18-32 | 15 | |
| β-strand | 35-39 | 5 | 1 |
| α-helix | 44-52 | 9 | |
| β-strand | 60-64 | 5 | 1 |
| α-helix | 65-67 | 3 | |
| α-helix | 68-73 | 6 | |
| β-strand | 77 | 1 | 2 |
| α-helix | 78-80 | 3 | |
| α-helix | 84-87 | 4 | |
| β-strand | 90 | 1 | 3 |
| α-helix | 92-97 | 6 | |
| β-strand | 99-100 | 2 | 4 |
| β-strand | 103-104 | 2 | 4 |
| β-strand | 107-112 | 6 | 1 |
| β-strand | 115-119 | 5 | 5 |
| β-strand | 129 | 1 | 6 |
| α-helix | 130-132 | 3 | |
| α-helix | 133-141 | 9 | |
| β-strand | 146-148 | 3 | 5 |
| α-helix | 155-157 | 3 | |
| α-helix | 159-164 | 6 | |
| β-strand | 168-173 | 6 | 7 |
| β-strand | 176-183 | 8 | 7 |
| α-helix | 187-201 | 15 | |
| α-helix | 211-219 | 9 | |
| β-strand | 223-228 | 6 | 5 |
| α-helix | 230-232 | 3 | |
| α-helix | 233-239 | 7 | |
| β-strand | 243-246 | 4 | 5 |
| α-helix | 247-249 | 3 | |
| β-strand | 250 | 1 | 6 |
| β-strand | 251 | 1 | 8 |
| β-strand | 254 | 1 | 8 |
| α-helix | 255-256 | 2 | |
| α-helix | 258 | 1 | |
| β-strand | 259-260 | 2 | 9 |
| β-strand | 261-267 | 7 | 1 |
| β-strand | 268 | 1 | 2 |
| α-helix | 274-280 | 7 | |
| α-helix | 281-285 | 5 | |
| α-helix | 288-297 | 10 | |
| β-strand | 302-303 | 2 | 1 |
| β-strand | 305 | 1 | 3 |
| α-helix | 306-312 | 7 | |
| α-helix | 316-327 | 12 | |
| β-strand | 329-330 | 2 | 9 |
| α-helix | 331-332 | 2 | |
| α-helix | 337-353 | 17 | |
| α-helix | 358-369 | 12 | |
| α-helix | 383-394 | 12 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Maltose-binding periplasmic protein/alpha-synuclein chimeric protein | A | protein | 404 | Escherichia coli, Homo sapiens | P0AEX9 (AlphaFold model), P37840 (AlphaFold model) |
>3Q26_1 Maltose-binding periplasmic protein/alpha-synuclein chimeric protein (chains A) MKIEEGKLVIWINGDKGYNGLAEVGKKFEKDTGIKVTVEHPDKLEEKFPQVAATGDGPDI IFWAHDRFGGYAQSGLLAEITPDKAFQDKLYPFTWDAVRYNGKLIAYPIAVEALSLIYNK DLLPNPPKTWEEIPALDKELKAKGKSALMFNLQEPYFTWPLIAADGGYAFKYENGKYDIK DVGVDNAGAKAGLTFLVDLIKNKHMNADTDYSIAEAAFNKGETAMTINGPWAWSNIDTSK VNYGVTVLPTFKGQPSKPFVGVLSAGINAASPNKELAKEFLENYLLTDEGLEAVNKDKPL GAVALKSYEEELAKDPRIAATMENAQKGEIMPNIPQMSAFWYAVRTAVINAASGRQTVDE ALKDAQTNSSSKAKEGVVAAAEKTKQGVAEAAGKTKEGVLYVGS
Structures of segments of alpha-synuclein fused to maltose-binding protein suggest intermediate states during amyloid formation. Zhao, M., Cascio, D., Sawaya, M.R. et al. Protein Sci (2011) 20:996-1004. DOI 10.1002/pro.630 · PubMed
Other PDB entries of the same protein (UniProt P0AEX9 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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