P18505: Gamma-aminobutyric acid receptor subunit beta-1 (GABRB1)

Gamma-aminobutyric acid receptor subunit beta-1 (GABRB1) is a 474-residue protein from Homo sapiens. This is its AlphaFold structure prediction, created 1 Aug 2025. UniProt accession: P18505.

Gene
GABRB1
Organism
Homo sapiens
Length
474 residues
Mean pLDDT
77.5
Model
AF-P18505-F1 v6
Model created
1 Aug 2025
PDB structures
3

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Model confidence (pLDDT)

The mean pLDDT of this model is 77.5 (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 caution8%
Below 50Very low: often disordered regions23%

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:10449790, PubMed:16412217, PubMed:26950270). GABA-gated chloride channels, also named GABA(A) receptors (GABAAR), consist of five subunits arranged around a central pore and contain one or two GABA active binding sites located at the alpha and beta subunit interfaces, depending on subunit composition (By similarity). When activated by GABA, GABAARs selectively allow the flow of chloride anions across the cell membrane down their electrochemical gradient (PubMed:10449790, PubMed:16412217, PubMed:26950270). Chloride influx into…

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:10449790, PubMed:16412217). Binds UBQLN1 (By similarity)

Subcellular location

Postsynaptic cell membrane, Cell membrane

Disease associations

Experimental structures in the PDB

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

PDB IDMethodResolutionChains and residues
9CXBEM3.33 ÅC=26-474
9CTVEM3.36 ÅD=26-474
9CXDEM3.36 ÅC/D=26-474

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