Human Apolipoprotein E4 (ApoE4) N-terminal domain (space group P212121). Determined by X-ray diffraction at 1.55 Å resolution. Released 30 Aug 2023.
Explore 8AX9 in 3D Show helices and sheets RCSB PDB PDBe
8AX9 contains 6 α-helices and 0 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 | 25-41 | 17 | |
| α-helix | 45-52 | 8 | |
| α-helix | 55-78 | 24 | |
| α-helix | 82-84 | 3 | |
| α-helix | 88-123 | 36 | |
| α-helix | 131-162 | 32 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Maltose/maltodextrin-binding periplasmic protein,Apolipoprotein E | A | protein | 675 | Homo sapiens | P02649 (AlphaFold model), P0AEX9 (AlphaFold model) |
>8AX9_1 Maltose/maltodextrin-binding periplasmic protein,Apolipoprotein E (chains A) GPMKIEEGKLVIWINGDKGYNGLAEVGKKFEKDTGIKVTVEHPDKLEEKFPQVAATGDGP DIIFWAHDRFGGYAQSGLLAEITPAAAFQDKLYPFTWDAVRYNGKLIAYPIAVEALSLIY NKDLLPNPPKTWEEIPALDKELKAKGKSALMFNLQEPYFTWPLIAADGGYAFKYENGKYD IKDVGVDNAGAKAGLTFLVDLIKNKHMNADTDYSIAEAAFNKGETAMTINGPWAWSNIDT SAVNYGVTVLPTFKGQPSKPFVGVLSAGINAASPNKELAKEFLENYLLTDEGLEAVNKDK PLGAVALKSYEEELAKDPRIAATMENAQKGEIMPNIPQMSAFWYAVRTAVINAASGRQTV DAALAAAQTNAAAAHMKVEQAVETEPEPELRQQTEWQSGQRWELALGRFWDYLRWVQTLS EQVQEELLSSQVTQELRALMDETMKELKAYKSELEEQLTPVAEETRARLSKELQAAQARL GADMEDVRGRLVQYRGEVQAMLGQSTEELRVRLASHLRKLRKRLLRDADDLQKRLAVYQA GAREGAERGLSAIRERLGPLVEQGRVRAATVGSLAGQPLQERAQAWGERLRARMEEMGSR TRDRLDEVKEQVAEVRAKLEEQAQQIRLQAEAAQARLKSRFEPLAEDMQRQWAGQVEKVQ AAEGTSAAPVPSDNH
Domino-like effect of C112R mutation on ApoE4 aggregation and its reduction by Alzheimer's Disease drug candidate. Nemergut, M., Marques, S.M., Uhrik, L. et al. Mol Neurodegener (2023) 18:38-38. DOI 10.1186/s13024-023-00620-9 · PubMed
Other PDB entries of the same protein (UniProt P02649 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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