8FRX: Full-length mouse 5-HT3A receptor

Full-length mouse 5-HT3A receptor in complex with SMP100, pre-activated. Determined by electron microscopy at 2.7 Å resolution. Released 27 Dec 2023.

Method: Electron microscopy
Resolution: 2.7 Å
Organism: Mus musculus
Chains: 5
Atoms: 16,670
Mol. weight: 316.55 kDa
Ligands: Y82, NAG
Released: 27 Dec 2023

Explore 8FRX in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

8FRX contains 70 α-helices and 55 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.

Chains A, B, C, D and E: 14 helices, 11 β-strands

Element	Residues	Length	Sheet
α-helix	13-20	8
α-helix	36	1
β-strand	37-52	16	1
β-strand	57-74	18	1
β-strand	85-89	5	1
α-helix	90-92	3
β-strand	98-100	3	2
β-strand	103	1	1
β-strand	114-118	5	1
β-strand	120-134	15	1
α-helix	142-144	3
β-strand	146-155	10	2
β-strand	163-167	5	1
α-helix	171-175	5
β-strand	187-199	13	2
β-strand	207-218	12	2
α-helix	220-223	4
α-helix	229-241	13
α-helix	251-270	20
α-helix	282-308	27
α-helix	315-317	3
α-helix	318-320	3
α-helix	322-326	5
α-helix	327-331	5
α-helix	398-460	63

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
5-hydroxytryptamine receptor 3A	A, B, C, D, E	protein	553	Mus musculus	P23979 (AlphaFold model)

Sequence of entity 1 (A, B, C, D, E), FASTA

>8FRX_1 5-hydroxytryptamine receptor 3A (chains A, B, C, D, E)
WSHPQFEKGGGSGGGSGGGSWSHPQFEKGGGSGGGSGGGSWSHPQFEKGGGSGGGSGGGS
WSHPQFEKENLYFQGATQARDTTQPALLRLSDHLLANYKKGVRPVRDWRKPTTVSIDVIM
YAILNVDEKNQVLTTYIWYRQYWTDEFLQWTPEDFDNVTKLSIPTDSIWVPDILINEFVD
VGKSPNIPYVYVHHRGEVQNYKPLQLVTACSLDIYNFPFDVQNCSLTFTSWLHTIQDINI
TLWRSPEEVRSDKSIFINQGEWELLEVFPQFKEFSIDISNSYAEMKFYVIIRRRPLFYAV
SLLLPSIFLMVVDIVGFCLPPDSGERVSFKITLLLGYSVFLIIVSDTLPATAIGTPLIGV
YFVVCMALLVISLAETIFIVRLVHKQDLQRPVPDWLRHLVLDRIAWILCLGEQPMAHRPP
ATFQANKTDDCSGSDLLPAMGNHCSHVGGPQDLEKTPRGRGSPLPPPREASLAVRGLLQE
LSSIRHFLEKRDEMREVARDWLRVGYVLDRLLFRIYLLAVLAYSITLVTLWSIWHYSENL
YFQGTETSQVAPA

Ligands and cofactors

ID	Name	Formula	Copies
Y82	5-[(1R,3S,4R)-1-azabicyclo[2.2.2]octan-3-yl]-1,3,4,5-tetrahydro-6H-azepino[5,4,…	C17 H20 N4 O	5
NAG	2-acetamido-2-deoxy-beta-D-glucopyranose	C8 H15 N O6	15

Primary citation

Structural basis for partial agonism in 5-HT 3A receptors. Felt, K., Stauffer, M., Salas-Estrada, L. et al. Nat Struct Mol Biol (2024) 31:598-609. DOI 10.1038/s41594-023-01140-2 · PubMed

Other PDB entries of the same protein (UniProt P23979 (AlphaFold model), which also has an AlphaFold model), best resolution first:

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)
6HIQ 3.2 Å, Mouse serotonin 5-HT3 receptor, serotonin-bound, I2 conformation

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