CryoEM structure of the alpha1AAR complex with doxazosin. Determined by electron microscopy at 2.99 Å resolution. Released 2 Jul 2025.
Explore 9M4Q in 3D Show helices and sheets RCSB PDB PDBe
9M4Q contains 14 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 | 24-53 | 30 | |
| α-helix | 60-74 | 15 | |
| α-helix | 75-79 | 5 | |
| α-helix | 80-89 | 10 | |
| α-helix | 96-129 | 34 | |
| α-helix | 134-137 | 4 | |
| α-helix | 140-159 | 20 | |
| α-helix | 167-170 | 4 | |
| α-helix | 182-189 | 8 | |
| α-helix | 190-194 | 5 | |
| α-helix | 195-213 | 19 | |
| α-helix | 262-297 | 36 | |
| α-helix | 305-329 | 25 | |
| α-helix | 331-340 | 10 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Alpha-1A adrenergic receptor | A | protein | 323 | Homo sapiens | P35348 (AlphaFold model) |
>9M4Q_1 Alpha-1A adrenergic receptor (chains A) APVNISKAILLGVILGGLILFGVLGNILVILSVACHRHLHSVTHYYIVNLAVADLLLTST VLPFSAIFEVLGYWAFGRVFCNIWAAVDVLCCTASIMGLCIISIDRYIGVSYPLRYPTIV TQRRGLMALLCVWALSLVISIGPLFGWRQPAPEDETICQINEEPGYVLFSALGSFYLPLA IILVMYCRVYVVAKRESRGLKSGLKTDKSDSEQVTLRIHRKNAPAGGSGMASAKTKTHFS VRLLKFSREKKAAKTLGIVVGCFVLCWLPFFLVMPIGSFFPDFKPSETVFKIVFWLGYLN SCINPIIYPCSSQEFKKAFQNVL
| ID | Name | Formula | Copies |
|---|---|---|---|
| A1EM4 | Doxazosin, (S)- | C23 H25 N5 O5 | 1 |
Molecular mechanism of antagonist recognition and regulation of the alpha 1A -adrenoceptor. Liu, S., Jiao, H., Tao, Y. et al. J Biol Chem (2025) 301:110348-110348. DOI 10.1016/j.jbc.2025.110348 · PubMed
Other PDB entries of the same protein (UniProt P35348 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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