P15431: Gamma-aminobutyric acid receptor subunit beta-1 (Gabrb1)

Gamma-aminobutyric acid receptor subunit beta-1 (Gabrb1) is a 474-residue protein from Rattus norvegicus. This is its AlphaFold structure prediction, created 1 Aug 2025. UniProt accession: P15431.

Gene
Gabrb1
Organism
Rattus norvegicus
Length
474 residues
Mean pLDDT
77.9
Model
AF-P15431-F1 v6
Model created
1 Aug 2025
PDB structures
3

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Model confidence (pLDDT)

The mean pLDDT of this model is 77.9 (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 accurate56%
70 to 90Confident: backbone generally right13%
50 to 70Low: treat with caution9%
Below 50Very low: often disordered regions22%

What pLDDT means and how to read it

Function

Beta subunit of the heteropentameric ligand-gated chloride channel gated by gamma-aminobutyric acid (GABA), a major inhibitory neurotransmitter in the brain (PubMed:1977069). GABA-gated chloride channels, also named GABA(A) receptors (GABAAR), consist of five subunits arranged around a central pore and contain GABA active binding site(s) located at the alpha and beta subunit interface(s) (PubMed:30044221). When activated by GABA, GABAARs selectively allow the flow of chloride anions across the cell membrane down their electrochemical gradient (PubMed:1977069). Chloride influx into the postsynaptic neuron following GABAAR opening decreases the neuron ability to generate a new action…

Subunit structure

Heteropentamer, formed by a combination of alpha (GABRA1-6), beta (GABRB1-3), gamma (GABRG1-3), delta (GABRD), epsilon (GABRE), rho (GABRR1-3), pi (GABRP) and theta (GABRQ) chains, each subunit exhibiting distinct physiological and pharmacological properties (PubMed:30044221). Binds UBQLN1 (By similarity)

Subcellular location

Postsynaptic cell membrane, Cell membrane

Experimental structures in the PDB

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

PDB IDMethodResolutionChains and residues
9OUOEM2.92 ÅB/E=1-474
6DW1EM3.1 ÅB/E=1-333, B/E=440-474
6DW0EM3.8 ÅB/E=1-333, B/E=440-474

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