5HT2BR-fab heterotrimer in complex with a novel antagonist IHCH-2330. Determined by electron microscopy at 2.98 Å resolution. Released 9 Sept 2026.
Explore 9WNG in 3D Show helices and sheets RCSB PDB PDBe
9WNG contains 28 α-helices and 44 β-strands across 3 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 | 4-7 | 4 | 1 |
| β-strand | 10-12 | 3 | 2 |
| β-strand | 19-25 | 7 | 1 |
| β-strand | 32-37 | 6 | 2 |
| β-strand | 44-48 | 5 | 2 |
| β-strand | 52-53 | 2 | 2 |
| β-strand | 61-65 | 5 | 1 |
| β-strand | 69-74 | 6 | 1 |
| α-helix | 79-81 | 3 | |
| β-strand | 84-89 | 6 | 2 |
| α-helix | 95 | 1 | |
| β-strand | 96 | 1 | 2 |
| β-strand | 101-104 | 4 | 2 |
| β-strand | 110 | 1 | 3 |
| β-strand | 113-117 | 5 | 4 |
| α-helix | 118-120 | 3 | |
| α-helix | 121-124 | 4 | |
| β-strand | 128-138 | 11 | 4 |
| β-strand | 139 | 1 | 3 |
| β-strand | 143-149 | 7 | 5 |
| β-strand | 153 | 1 | 5 |
| β-strand | 162 | 1 | 4 |
| α-helix | 163-166 | 4 | |
| β-strand | 172-181 | 10 | 4 |
| α-helix | 182-186 | 5 | |
| β-strand | 190-197 | 8 | 5 |
| β-strand | 205-209 | 5 | 5 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 3-6 | 4 | 6 |
| α-helix | 7-9 | 3 | |
| β-strand | 10-12 | 3 | 7 |
| β-strand | 18 | 1 | 6 |
| β-strand | 21-25 | 5 | 6 |
| α-helix | 29-31 | 3 | |
| β-strand | 34-40 | 7 | 7 |
| β-strand | 44-51 | 8 | 7 |
| β-strand | 58-60 | 3 | 7 |
| α-helix | 62-64 | 3 | |
| β-strand | 68-73 | 6 | 6 |
| β-strand | 78-83 | 6 | 6 |
| α-helix | 88-90 | 3 | |
| β-strand | 92-98 | 7 | 7 |
| β-strand | 101-104 | 4 | 8 |
| β-strand | 109-112 | 4 | 8 |
| β-strand | 116-117 | 2 | 7 |
| β-strand | 121-125 | 5 | 7 |
| β-strand | 134-137 | 4 | 9 |
| β-strand | 150-157 | 8 | 9 |
| β-strand | 164-168 | 5 | 10 |
| β-strand | 173 | 1 | 10 |
| β-strand | 177-179 | 3 | 9 |
| α-helix | 180-182 | 3 | |
| β-strand | 193-198 | 6 | 9 |
| α-helix | 200-202 | 3 | |
| β-strand | 209-214 | 6 | 10 |
| α-helix | 215-217 | 3 | |
| β-strand | 219-224 | 6 | 10 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 57-81 | 25 | |
| α-helix | 88-102 | 15 | |
| α-helix | 103-107 | 5 | |
| α-helix | 108-116 | 9 | |
| α-helix | 127-156 | 30 | |
| α-helix | 169-187 | 19 | |
| α-helix | 189-192 | 4 | |
| β-strand | 195-197 | 3 | 8 |
| α-helix | 202-204 | 3 | |
| α-helix | 216-222 | 7 | |
| α-helix | 223-227 | 5 | |
| α-helix | 228-243 | 16 | |
| α-helix | 323-349 | 27 | |
| α-helix | 355-377 | 23 | |
| α-helix | 378-382 | 5 | |
| α-helix | 385-393 | 9 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| P2C2 Fab light chain | B | protein | 236 | Homo sapiens | |
| P2C2 Fab heavy chain | C | protein | 270 | Homo sapiens | |
| 5-hydroxytryptamine receptor 2B | R | protein | 307 | Homo sapiens | P41595 (AlphaFold model) |
>9WNG_1 P2C2 Fab light chain (chains B) MKKNIAFLLASMFVFSIATNAYADIVLIQSPAIMSASPGEKVTITCSASSSVSYMHWFQQ KPGTSPKLWIYSTSNLASGVPARFSGSGSGTSYSLTISRMEAEDAATYYCQQRSSYPLTF GAGTKLEIKRTVAAPSVFIFPPSDEQLKSGTASVVCLLNNFYPREAKVQWKVDNALQSGN SQESVTEQDSKDSTYSLSSTLTLSKADYEKHKVYACEVTHQGLSLPVTKSFNRGEC
>9WNG_2 P2C2 Fab heavy chain (chains C) MKKNIAFLLASMFVFSIATNAYAEVQLQQSGPELVKPGASVKLSCKASGYTFTSSWMHWV KQRPGQGLEWIGNIYPSNGGTNYNERFKSKATLTVDRSSNTAYMQLSSLTSEDSAVYFCA RFGSFITTILTTYYNPVDYWGQGTTLTVSSASTKGPSVFPLAPSSKSTSGGTAALGCLVK DYFPEPVTVSWNSGALTSGVHTFPAVLQSSGLYSLSSVVTVPSSSLGTQTYICNVNHKPS NTKVDKKVEPKSCENLYFQSGSHHHHHHHH
>9WNG_3 5-hydroxytryptamine receptor 2B (chains R) GPGSGSGTESIPEEMKQIVEEQGNKLHWAALLILMVIIPTIGGNTLVILAVSLEKKLQYA TNYFLMSLAVADLLVGLFVMPIALLTIMFEAMWPLPLVLCPAWLFLDVLFSTASIWHLCA ISVDRYIAIKKPIQANQYNSRATAFIKITVVWLISIGIAIPVPIKGIETDVDNPNNITCV LTKERFGDFMLFGSLAAFFTPLAIMIVTYFLTIHALQKKRLLSGSRQTISNEQRASKVLG IVFFLFLLMWCPFFITNITLVLCDSCNQTTLQMLLEIFVWIGYVSSGVNPLVYTLFNKTF RDAFGRY
| ID | Name | Formula | Copies |
|---|---|---|---|
| NAG | 2-acetamido-2-deoxy-beta-D-glucopyranose | C8 H15 N O6 | 1 |
| A1EXY | 3-[2-[2-[2,5-dimethoxy-4-(trifluoromethyl)phenyl]ethyl-methyl-amino]ethyl]-2-me… | C23 H26 F3 N3 O3 | 1 |
Mechanistic Basis for 5-HT 2A R Over 5-HT 2B R Activation. Tang, L., Ji, X., Wang, Y. et al. Nat Commun (2026) 17. DOI 10.1038/s41467-026-77659-x · PubMed
Other PDB entries of the same protein (UniProt P41595 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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