9AS8: Global reconstruction of 5-HT2AR
Global reconstruction of 5-HT2AR bound to psilocin in complex with a mini-Gq protein and scFv16 obtained by cryo-electron microscopy (cryoEM). Determined by electron microscopy at 2.54 Å resolution. Released 2 Apr 2025.
- Method
- Electron microscopy
- Resolution
- 2.54 Å
- Organism
- Homo sapiens
- Chains
- 5
- Atoms
- 8,257
- Mol. weight
- 156.89 kDa
- Ligands
- 91Q
- Released
- 2 Apr 2025
Explore 9AS8 in 3D
Show helices and sheets
RCSB PDB
PDBe
Secondary structure: helices and β-sheets
9AS8 contains 32 α-helices and 64 β-strands across 5 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.
Chain A: 15 helices, 2 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 82-101 | 20 | |
| α-helix | 103-105 | 3 | |
| α-helix | 108-122 | 15 | |
| α-helix | 123-127 | 5 | |
| α-helix | 128-136 | 9 | |
| α-helix | 147-178 | 32 | |
| α-helix | 180-186 | 7 | |
| α-helix | 189-207 | 19 | |
| α-helix | 209-214 | 6 | |
| α-helix | 218-220 | 3 | |
| β-strand | 222-223 | 2 | 1 |
| β-strand | 226-227 | 2 | 1 |
| α-helix | 232-240 | 9 | |
| α-helix | 245-260 | 16 | |
| α-helix | 315-348 | 34 | |
| α-helix | 355-381 | 27 | |
| α-helix | 385-391 | 7 | |
Chain B: 8 helices, 7 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 7-31 | 25 | |
| β-strand | 34-40 | 7 | 2 |
| β-strand | 70-76 | 7 | 2 |
| β-strand | 79-85 | 7 | 2 |
| α-helix | 95-100 | 6 | |
| β-strand | 105-111 | 7 | 2 |
| α-helix | 118-129 | 12 | |
| β-strand | 138-144 | 7 | 2 |
| α-helix | 146-155 | 10 | |
| α-helix | 160-163 | 4 | |
| α-helix | 165-168 | 4 | |
| α-helix | 184-204 | 21 | |
| β-strand | 211 | 1 | 2 |
| β-strand | 214-215 | 2 | 2 |
| α-helix | 224-242 | 19 | |
Chain C: 3 helices, 28 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 4-25 | 22 | |
| α-helix | 30-33 | 4 | |
| β-strand | 47-51 | 5 | 3 |
| β-strand | 58-63 | 6 | 4 |
| β-strand | 69-74 | 6 | 4 |
| β-strand | 78-83 | 6 | 4 |
| β-strand | 89-94 | 6 | 4 |
| β-strand | 100-105 | 6 | 5 |
| β-strand | 111-116 | 6 | 5 |
| β-strand | 121-125 | 5 | 5 |
| β-strand | 134-139 | 6 | 5 |
| β-strand | 146-151 | 6 | 6 |
| β-strand | 156-161 | 6 | 6 |
| β-strand | 166-170 | 5 | 6 |
| β-strand | 175-180 | 6 | 6 |
| β-strand | 187-192 | 6 | 7 |
| β-strand | 198-203 | 6 | 7 |
| β-strand | 208-212 | 5 | 7 |
| β-strand | 218-222 | 5 | 7 |
| β-strand | 229-234 | 6 | 8 |
| β-strand | 240-245 | 6 | 8 |
| β-strand | 250-254 | 5 | 8 |
| β-strand | 259-264 | 6 | 8 |
| α-helix | 272 | 1 | |
| β-strand | 273-278 | 6 | 9 |
| β-strand | 284-289 | 6 | 9 |
| β-strand | 294-298 | 5 | 9 |
| β-strand | 304-308 | 5 | 9 |
| β-strand | 315-320 | 6 | 3 |
| β-strand | 327-331 | 5 | 3 |
| β-strand | 336-339 | 4 | 3 |
Chain D: 2 helices, 0 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 10-23 | 14 | |
| α-helix | 30-43 | 14 | |
Chain E: 4 helices, 27 β-strands
| Element | Residues | Length | Sheet |
|---|
| β-strand | 3-7 | 5 | 10 |
| β-strand | 10-11 | 2 | 11 |
| β-strand | 18-25 | 8 | 10 |
| α-helix | 29-31 | 3 | |
| β-strand | 33-34 | 2 | 12 |
| β-strand | 38-39 | 2 | 11 |
| β-strand | 45-46 | 2 | 11 |
| β-strand | 49-51 | 3 | 12 |
| β-strand | 58-60 | 3 | 12 |
| β-strand | 68-73 | 6 | 10 |
| β-strand | 78-83 | 6 | 10 |
| α-helix | 88-90 | 3 | |
| β-strand | 92-94 | 3 | 11 |
| β-strand | 97-99 | 3 | 12 |
| β-strand | 110-111 | 2 | 12 |
| β-strand | 115-118 | 4 | 11 |
| β-strand | 128-129 | 2 | 13 |
| β-strand | 134-136 | 3 | 14 |
| β-strand | 143-149 | 7 | 13 |
| β-strand | 154 | 1 | 15 |
| β-strand | 160 | 1 | 15 |
| β-strand | 162-167 | 6 | 14 |
| β-strand | 174-178 | 5 | 14 |
| β-strand | 182-183 | 2 | 14 |
| α-helix | 184 | 1 | |
| β-strand | 191-196 | 6 | 13 |
| β-strand | 199-204 | 6 | 13 |
| β-strand | 213-219 | 7 | 14 |
| α-helix | 225 | 1 | |
| β-strand | 226-227 | 2 | 14 |
| β-strand | 231-234 | 4 | 14 |
Molecules and chains
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|
| 5-hydroxytryptamine receptor 2A | A | protein | 471 | Homo sapiens | P28223 (AlphaFold model) |
| G subunit q (Gi2-mini-Gq chimeric) | B | protein | 246 | Homo sapiens | |
| Guanine nucleotide-binding protein G(I)/G(S)/G(T) subunit beta-1 | C | protein | 358 | Homo sapiens | P62873 (AlphaFold model) |
| Guanine nucleotide-binding protein G(I)/G(S)/G(O) subunit gamma-2 | D | protein | 71 | Homo sapiens | P59768 (AlphaFold model) |
| single chain Fab (svFv16) | E | protein | 267 | Homo sapiens | |
Sequence of entity 1 (A), FASTA
>9AS8_1 5-hydroxytryptamine receptor 2A (chains A)
MDILCEENTSLSSTTNSLMQLNDDTRLYSNDFNSGEANTSDAFNWTVDSENRTNLSCEGC
LSPSCLSLLHLQEKNWSALLTAVVIILTIAGNILVIMAVSLEKKLQNATNYFLMSLAIAD
MLLGFLVMPVSMLTILYGYRWPLPSKLCAVWIYLDVLFSTASIMHLCAISLDRYVAIQNP
IHHSRFNSRTKAFLKIIAVWTISVGISMPIPVFGLQDDSKVFKEGSCLLADDNFVLIGSF
VSFFIPLTIMVITYFLTIKSLQKEATLCVSDLGTRAKLASFSFLPQSSLSSEKLFQRSIH
REPGSYTGRRTMQSISNEQKACKVLGIVFFLFVVMWCPFFITNIMAVICKESCNEDVIGA
LLNVFVWIGYLSSAVNPLVYTLFNKTYRSAFSRYIQCQYKENKKPLQLILVNTIPALAYK
SSQLQMGQKKNSKQDAKTTDNDCSMVALGKQHSEEASKDNSDGVNEKVSCV
Sequence of entity 2 (B), FASTA
>9AS8_2 G subunit q (Gi2-mini-Gq chimeric) (chains B)
MGSTVSAEDKAAAERSKMIDKNLREDGEKARRTLRLLLLGADNSGKSTIVKQMRILHGGS
GGSGGTSGIFETKFQVDKVNFHMFDVGGQRDERRKWIQCFNDVTAIIFVVDSSDYNRLQE
ALNDFKSIWNNRWLRTISVILFLNKQDLLAEKVLAGKSKIEDYFPEFARYTTPEDATPEP
GEDPRVTRAKYFIRKEFVDISTASGDGRHICYPHFTCAVDTENARRIFNDCKDIILQMNL
REYNLV
Sequence of entity 3 (C), FASTA
>9AS8_3 Guanine nucleotide-binding protein G(I)/G(S)/G(T) subunit beta-1 (chains C)
MHHHHHHLEVLFQGPGSSGSELDQLRQEAEQLKNQIRDARKACADATLSQITNNIDPVGR
IQMRTRRTLRGHLAKIYAMHWGTDSRLLVSASQDGKLIIWDSYTTNKVHAIPLRSSWVMT
CAYAPSGNYVACGGLDNICSIYNLKTREGNVRVSRELAGHTGYLSCCRFLDDNQIVTSSG
DTTCALWDIETGQQTTTFTGHTGDVMSLSLAPDTRLFVSGACDASAKLWDVREGMCRQTF
TGHESDINAICFFPNGNAFATGSDDATCRLFDLRADQELMTYSHDNIICGITSVSFSKSG
RLLLAGYDDFNCNVWDALKADRAGVLAGHDNRVSCLGVTDDGMAVATGSWDSFLKIWN
Sequence of entity 4 (D), FASTA
>9AS8_4 Guanine nucleotide-binding protein G(I)/G(S)/G(O) subunit gamma-2 (chains D)
MASNNTASIAQARKLVEQLKMEANIDRIKVSKAAADLMAYCEAHAKEDPLLTPVPASENP
FREKKFFCAIL
Sequence of entity 5 (E), FASTA
>9AS8_5 single chain Fab (svFv16) (chains E)
DVQLVESGGGLVQPGGSRKLSCSASGFAFSSFGMHWVRQAPEKGLEWVAYISSGSGTIYY
ADTVKGRFTISRDDPKNTLFLQMTSLRSEDTAMYYCVRSIYYYGSSPFDFWGQGTTLTVS
SGGGGSGGGGSGGGGSDIVMTQATSSVPVTPGESVSISCRSSKSLLHSNGNTYLYWFLQR
PGQSPQLLIYRMSNLASGVPDRFSGSGSGTAFTLTISRLEAEDVGVYYCMQHLEYPLTFG
AGTKLELKAAALEVLFQGPHHHHHHHH
Ligands and cofactors
| ID | Name | Formula | Copies |
|---|
| 91Q | 3-[2-(dimethylamino)ethyl]-1~{H}-indol-4-ol | C12 H16 N2 O | 1 |
Primary citation
The structural diversity of psychedelic drug actions revealed. Gumpper, R.H., Jain, M.K., Kim, K. et al. Nat Commun (2025) 16:2734-2734. DOI 10.1038/s41467-025-57956-7 · PubMed
Other PDB entries of the same protein (UniProt P28223 (AlphaFold model), which also has an AlphaFold model), best resolution first:
- 7WC8 2.45 Å, Crystal structure of serotonin 2A receptor in complex with lumateperone
- 7WC9 2.5 Å, Crystal structure of serotonin 2A receptor in complex with non-hallucinogenic…
- 7WC6 2.6 Å, Crystal structure of serotonin 2A receptor in complex with LSD
- 7WC7 2.6 Å, Crystal structure of serotonin 2A receptor in complex with lisuride
- 9LL8 2.62 Å, Psilocin-bound Serotonin 2A (5-HT2A) receptor-Gi complex
- 8JT8 2.7 Å, Crystal structure of 5-HT2AR in complex with (R)-IHCH-7179
- 9AS7 2.72 Å, Local refinement of 5-HT2AR bound to psilocin in complex with a mini-Gq and scFv16…
- 9LL9 2.76 Å, DOI-bound Serotonin 2A (5-HT2A) receptor-Gq complex
- 8UWL 2.8 Å, 5-HT2AR bound to Lisuride in complex with a mini-Gq protein and an active-state…
- 9J87 2.84 Å, Structure of Receptor
- 9LL7 2.84 Å, DOI-bound Serotonin 2A (5-HT2A) receptor-Gi complex
- 6A94 2.9 Å, Crystal structure of 5-HT2AR in complex with zotepine
Browse structure collections
About this viewer
MolViewer shows 9AS8 directly in your browser with nothing to install. Switch between cartoon, ball-and-stick, spacefill and surface views, color by chain, secondary structure or B-factor, measure distances, angles and dihedrals, and share or embed the view.