P30926: Neuronal acetylcholine receptor subunit beta-4 (CHRNB4)

Neuronal acetylcholine receptor subunit beta-4 (CHRNB4) is a 498-residue protein from Homo sapiens. This is its AlphaFold structure prediction, created 1 Aug 2025. UniProt accession: P30926.

Gene
CHRNB4
Organism
Homo sapiens
Length
498 residues
Mean pLDDT
81.3
Model
AF-P30926-F1 v6
Model created
1 Aug 2025
PDB structures
4

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Model confidence (pLDDT)

The mean pLDDT of this model is 81.3 (confident overall). pLDDT is AlphaFold's per-residue confidence score from 0 to 100. In MolViewer, choose the B-factor color scheme to color the model by pLDDT, because AlphaFold stores it in the B-factor column.

pLDDT bandMeaningShare of residues
Above 90Very high: backbone and side chains are usually accurate61%
70 to 90Confident: backbone generally right17%
50 to 70Low: treat with caution6%
Below 50Very low: often disordered regions17%

What pLDDT means and how to read it

Function

Component of neuronal acetylcholine receptors (nAChRs) that function as pentameric, ligand-gated cation channels with high calcium permeability among other activities. nAChRs are excitatory neurotrasnmitter receptors formed by a collection of nAChR subunits known to mediate synaptic transmission in the nervous system and the neuromuscular junction. Each nAchR subunit confers differential attributes to channel properties, including activation, deactivation and desensitization kinetics, pH sensitivity, cation permeability, and binding to allosteric modulators (PubMed:20881005, PubMed:31488329, PubMed:8663494, PubMed:8906617, PubMed:9203638). CHRNB4 forms heteropentameric neuronal…

Subunit structure

Neuronal AChR is composed of two different types of subunits: alpha and beta. CHRNB4/Beta-4 subunit can be combined to CHRNA2/alpha-2, CHRNA3/alpha-3 or CHRNA4/alpha-4, CHRNA5/alpha-5 and CHRNB3/beta-3 to give rise to functional receptors (PubMed:11118490, PubMed:20881005, PubMed:31488329, PubMed:8663494, PubMed:8906617). Forms stoichiometries such as (CHRNA3)2:(CHRNB4)3 or…

Subcellular location

Synaptic cell membrane, Cell membrane

Experimental structures in the PDB

Compare the prediction with experimentally determined structures of the same protein:

PDB IDMethodResolutionChains and residues
8ZRNEM3.25 ÅB/D/E=1-498
8ZRPEM3.32 ÅB/D/E=1-498
6PV7EM3.34 ÅB/C/E=22-498
6PV8EM3.87 ÅB/C/E=22-498

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