4PIR: Mouse serotonin 5-HT3 receptor
X-ray structure of the mouse serotonin 5-HT3 receptor. Determined by X-ray diffraction at 3.5 Å resolution. Released 6 Aug 2014.
- Method
- X-ray diffraction
- Resolution
- 3.5 Å
- Organisms
- Mus musculus, Lama glama
- Chains
- 10
- Atoms
- 20,739
- Mol. weight
- 338 kDa
- Ligands
- NAG
- Released
- 6 Aug 2014
Explore 4PIR in 3D
Show helices and sheets
RCSB PDB
PDBe
Secondary structure: helices and β-sheets
4PIR contains 65 α-helices and 120 β-strands across 10 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.
Chains A and B: 12 helices, 12 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 12-20 | 9 | |
| α-helix | 36 | 1 | |
| β-strand | 37-52 | 16 | 1 |
| β-strand | 57-69 | 13 | 1 |
| β-strand | 85-89 | 5 | 1 |
| α-helix | 90-92 | 3 | |
| β-strand | 98-100 | 3 | 2 |
| β-strand | 103 | 1 | 1 |
| α-helix | 110-112 | 3 | |
| β-strand | 114-118 | 5 | 1 |
| β-strand | 122-134 | 13 | 1 |
| β-strand | 146-155 | 10 | 2 |
| β-strand | 163-167 | 5 | 1 |
| α-helix | 171-176 | 6 | |
| β-strand | 187-199 | 13 | 2 |
| β-strand | 203 | 1 | 3 |
| β-strand | 207-218 | 12 | 2 |
| α-helix | 222-242 | 21 | |
| α-helix | 250-268 | 19 | |
| α-helix | 285-307 | 23 | |
| α-helix | 318-321 | 4 | |
| α-helix | 322-328 | 7 | |
| α-helix | 329-333 | 5 | |
| α-helix | 403-457 | 55 | |
Chain C: 12 helices, 12 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 12-20 | 9 | |
| α-helix | 36 | 1 | |
| β-strand | 37-52 | 16 | 7 |
| β-strand | 57-69 | 13 | 7 |
| β-strand | 85-89 | 5 | 7 |
| α-helix | 90-92 | 3 | |
| β-strand | 98-100 | 3 | 8 |
| β-strand | 103 | 1 | 7 |
| α-helix | 110-112 | 3 | |
| β-strand | 114-118 | 5 | 7 |
| β-strand | 122-134 | 13 | 7 |
| β-strand | 146-155 | 10 | 8 |
| β-strand | 163-167 | 5 | 7 |
| α-helix | 171-176 | 6 | |
| β-strand | 187-200 | 14 | 8 |
| β-strand | 203 | 1 | 9 |
| β-strand | 206-218 | 13 | 8 |
| α-helix | 222-242 | 21 | |
| α-helix | 250-268 | 19 | |
| α-helix | 285-307 | 23 | |
| α-helix | 318-321 | 4 | |
| α-helix | 322-328 | 7 | |
| α-helix | 329-333 | 5 | |
| α-helix | 403-458 | 56 | |
Chain D: 12 helices, 12 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 12-20 | 9 | |
| α-helix | 36 | 1 | |
| β-strand | 37-52 | 16 | 10 |
| β-strand | 57-69 | 13 | 10 |
| β-strand | 85-89 | 5 | 10 |
| α-helix | 90-92 | 3 | |
| β-strand | 98-100 | 3 | 11 |
| β-strand | 103 | 1 | 10 |
| α-helix | 110-112 | 3 | |
| β-strand | 114-118 | 5 | 10 |
| β-strand | 122-134 | 13 | 10 |
| β-strand | 146-155 | 10 | 11 |
| β-strand | 163-167 | 5 | 10 |
| α-helix | 171-176 | 6 | |
| β-strand | 187-199 | 13 | 11 |
| β-strand | 203 | 1 | 12 |
| β-strand | 207-218 | 12 | 11 |
| α-helix | 222-242 | 21 | |
| α-helix | 250-268 | 19 | |
| α-helix | 285-307 | 23 | |
| α-helix | 318-321 | 4 | |
| α-helix | 322-328 | 7 | |
| α-helix | 329-333 | 5 | |
| α-helix | 403-458 | 56 | |
Chain E: 12 helices, 12 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 12-20 | 9 | |
| α-helix | 36 | 1 | |
| β-strand | 37-52 | 16 | 13 |
| β-strand | 57-69 | 13 | 13 |
| β-strand | 85-89 | 5 | 13 |
| α-helix | 90-92 | 3 | |
| β-strand | 98-100 | 3 | 14 |
| β-strand | 103 | 1 | 13 |
| α-helix | 110-112 | 3 | |
| β-strand | 114-118 | 5 | 13 |
| β-strand | 122-134 | 13 | 13 |
| β-strand | 146-155 | 10 | 14 |
| β-strand | 163-167 | 5 | 13 |
| α-helix | 171-176 | 6 | |
| β-strand | 187-202 | 16 | 14 |
| β-strand | 203 | 1 | 15 |
| β-strand | 205-218 | 14 | 14 |
| α-helix | 222-242 | 21 | |
| α-helix | 250-268 | 19 | |
| α-helix | 285-307 | 23 | |
| α-helix | 318-321 | 4 | |
| α-helix | 322-328 | 7 | |
| α-helix | 329-333 | 5 | |
| α-helix | 403-457 | 55 | |
Chain F: 1 helix, 12 β-strands
| Element | Residues | Length | Sheet |
|---|
| β-strand | 3-7 | 5 | 16 |
| β-strand | 11 | 1 | 17 |
| β-strand | 18-25 | 8 | 16 |
| β-strand | 29-39 | 11 | 3 |
| β-strand | 45-53 | 9 | 3 |
| β-strand | 60-64 | 5 | 3 |
| β-strand | 72-77 | 6 | 16 |
| β-strand | 82-87 | 6 | 16 |
| α-helix | 92-94 | 3 | |
| β-strand | 96-106 | 11 | 3 |
| β-strand | 110-114 | 5 | 3 |
| β-strand | 118-120 | 3 | 3 |
| β-strand | 121 | 1 | 17 |
Chains G, I and J: 1 helix, 12 β-strands
| Element | Residues | Length | Sheet |
|---|
| β-strand | 3-7 | 5 | 18 |
| β-strand | 11-12 | 2 | 19 |
| β-strand | 18-25 | 8 | 18 |
| β-strand | 29-39 | 11 | 6 |
| β-strand | 45-53 | 9 | 6 |
| β-strand | 60-64 | 5 | 6 |
| β-strand | 72-77 | 6 | 18 |
| β-strand | 82-87 | 6 | 18 |
| α-helix | 92-94 | 3 | |
| β-strand | 96-106 | 11 | 6 |
| β-strand | 110-114 | 5 | 6 |
| β-strand | 118-120 | 3 | 6 |
| β-strand | 121-122 | 2 | 19 |
Chain H: 1 helix, 12 β-strands
| Element | Residues | Length | Sheet |
|---|
| β-strand | 3-7 | 5 | 20 |
| β-strand | 11-12 | 2 | 21 |
| β-strand | 18-25 | 8 | 20 |
| β-strand | 30-39 | 10 | 9 |
| β-strand | 45-53 | 9 | 9 |
| β-strand | 60-64 | 5 | 9 |
| β-strand | 72-77 | 6 | 20 |
| β-strand | 82-87 | 6 | 20 |
| α-helix | 92-94 | 3 | |
| β-strand | 96-105 | 10 | 9 |
| β-strand | 110-114 | 5 | 9 |
| β-strand | 118-120 | 3 | 9 |
| β-strand | 121-122 | 2 | 21 |
Molecules and chains
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|
| 5-hydroxytryptamine receptor 3A | A, B, C, D, E | protein | 456 | Mus musculus | P23979 (AlphaFold model) |
| VHH15 | F, G, H, I, J | protein | 124 | Lama glama | |
Sequence of entity 1 (A, B, C, D, E), FASTA
>4PIR_1 5-hydroxytryptamine receptor 3A (chains A, B, C, D, E)
ATQARDTTQPALLRLSDHLLANYKKGVRPVRDWRKPTTVSIDVIMYAILNVDEKNQVLTT
YIWYRQYWTDEFLQWTPEDFDNVTKLSIPTDSIWVPDILINEFVDVGKSPNIPYVYVHHR
GEVQNYKPLQLVTACSLDIYNFPFDVQNCSLTFTSWLHTIQDINITLWRSPEEVRSDKSI
FINQGEWELLEVFPQFKEFSIDISNSYAEMKFYVIIRRRPLFYAVSLLLPSIFLMVVDIV
GFCLPPDSGERVSFKITLLLGYSVFLIIVSDTLPATAIGTPLIGVYFVVCMALLVISLAE
TIFIVRLVHKQDLQRPVPDWLRHLVLDRIAWILCLGEQPMAHRPPATFQANKTDDCSAMG
NHCSHVGGPQDLEKTPRGRGSPLPPPREASLAVRGLLQELSSIRHFLEKRDEMREVARDW
LRVGYVLDRLLFRIYLLAVLAYSITLVTLWSIWHSS
Sequence of entity 2 (F, G, H, I, J), FASTA
>4PIR_2 VHH15 (chains F, G, H, I, J)
DVQLVESGGGLVQPGGSLRLSCAYSGSLFSILRMDWYRQAPGKERELVAGITRDAAGYAD
STNYADSVKGRFTISRDSAKNTVYLQMNSLKPEDTAVYYCNADARTITGRADYWGQGTQV
TVSS
Ligands and cofactors
| ID | Name | Formula | Copies |
|---|
| NAG | 2-acetamido-2-deoxy-beta-D-glucopyranose | C8 H15 N O6 | 2 |
Water and common crystallization additives (SO4, CL) are not listed.
Primary citation
X-ray structure of the mouse serotonin 5-HT3 receptor. Hassaine, G., Deluz, C., Grasso, L. et al. Nature (2014) 512:276-281. DOI 10.1038/nature13552 · PubMed
Other PDB entries of the same protein (UniProt P23979 (AlphaFold model), which also has an AlphaFold model), best resolution first:
- 8FRX 2.7 Å, Full-length mouse 5-HT3A receptor in complex with SMP100, pre-activated
- 8FRZ 2.75 Å, Full-length mouse 5-HT3A receptor in complex with serotonin, pre-activated
- 8FSB 2.75 Å, Full-length mouse 5-HT3A receptor in complex with serotonin, open-like
- 6Y5A 2.8 Å, Serotonin-bound 5-HT3A receptor in Salipro
- 6Y1Z 2.82 Å, Mouse serotonin 5HT3 receptor in complex with palonosetron
- 6NP0 2.92 Å, Cryo-EM structure of 5HT3A receptor in presence of granisetron
- 6W1J 2.92 Å, Cryo-EM structure of 5HT3A receptor in presence of Alosetron
- 8FRW 2.92 Å, Full-length mouse 5-HT3A receptor in complex with ALB148471, pre-activated
- 8CC7 3.0 Å, Mouse serotonin 5-HT3A receptor in complex with PZ-1939
- 8AW2 3.01 Å, Mouse serotonin 5-HT3A receptor in complex with vortioxetine
- 6W1M 3.06 Å, Cryo-EM structure of 5HT3A receptor in presence of Ondansetron
- 6Y5B 3.1 Å, 5-HT3A receptor in Salipro (apo, asymmetric)
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