8AW2: Mouse serotonin 5-HT3A receptor

Mouse serotonin 5-HT3A receptor in complex with vortioxetine. Determined by electron microscopy at 3.01 Å resolution. Released 6 Mar 2024.

Method: Electron microscopy
Resolution: 3.01 Å
Organism: Mus musculus
Chains: 5
Atoms: 16,375
Mol. weight: 326.66 kDa
Ligands: NAG, VTX
Released: 6 Mar 2024

Explore 8AW2 in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

8AW2 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	11-20	10
β-strand	37-52	16	1
β-strand	57-69	13	1
α-helix	77-79	3
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	122-134	13	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	187-200	14	2
β-strand	206-218	13	2
α-helix	220-222	3
α-helix	224-228	5
α-helix	229-241	13
α-helix	246-248	3
α-helix	250-269	20
α-helix	282-308	27
α-helix	314-318	5
α-helix	319-326	8
α-helix	400-459	60

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
5-hydroxytryptamine receptor 3A	A, B, C, D, E	protein	566	Mus musculus	P23979 (AlphaFold model)

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

>8AW2_1 5-hydroxytryptamine receptor 3A (chains A, B, C, D, E)
MRLCIPQVLLALFLSMLTGPGEGSRRRWSHPQFEKGGGSGGGSGGGSWSHPQFEKGGGSG
GGSGGGSWSHPQFEKGGGSGGGSGGGSWSHPQFEKENLYFQGSGATQARDTTQPALLRLS
DHLLANYKKGVRPVRDWRKPTTVSIDVIMYAILNVDEKNQVLTTYIWYRQYWTDEFLQWT
PEDFDNVTKLSIPTDSIWVPDILINEFVDVGKSPNIPYVYVHHRGEVQNYKPLQLVTACS
LDIYNFPFDVQNCSLTFTSWLHTIQDINITLWRSPEEVRSDKSIFINQGEWELLEVFPQF
KEFSIDISNSYAEMKFYVIIRRRPLFYAVSLLLPSIFLMVVDIVGFCLPPDSGERVSFKI
TLLLGYSVFLIIVSDTLPATAIGTPLIGVYFVVCMALLVISLAETIFIVRLVHKQDLQRP
VPDWLRHLVLDRAAWILCLGEQPMAHRPPATFQANKTDDCSGSDLLPAMGNHCSHVGGPQ
DLEKTPRGRGSPLPPPREASLAVRGLLQELSSIRHFLEKRDEMREVARDWLRVGYVLDRL
LFRIYLLAVLAYSITLVTLWSIWHLW

Ligands and cofactors

ID	Name	Formula	Copies
NAG	2-acetamido-2-deoxy-beta-D-glucopyranose	C8 H15 N O6	5
VTX	Vortioxetine	C18 H22 N2 S	5

Water and common crystallization additives (CL) are not listed.

Primary citation

Structural determinants for activity of the antidepressant vortioxetine at human and rodent 5-HT 3 receptors. Lopez-Sanchez, U., Munro, L.J., Ladefoged, L.K. et al. Nat Struct Mol Biol (2024) 31:1232-1242. DOI 10.1038/s41594-024-01282-x · 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
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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