Gamma-aminobutyric acid type B receptor subunit 1 (GABBR1) is a 961-residue protein from Homo sapiens. This is its AlphaFold structure prediction, created 1 Aug 2025. UniProt accession: Q9UBS5.
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The mean pLDDT of this model is 84.2 (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 band | Meaning | Share of residues |
|---|---|---|
| Above 90 | Very high: backbone and side chains are usually accurate | 55% |
| 70 to 90 | Confident: backbone generally right | 30% |
| 50 to 70 | Low: treat with caution | 5% |
| Below 50 | Very low: often disordered regions | 10% |
What pLDDT means and how to read it
Component of a heterodimeric G protein-coupled receptor for GABA, formed by GABBR1 and GABBR2 (PubMed:15617512, PubMed:18165688, PubMed:22660477, PubMed:24305054, PubMed:36103875, PubMed:9872316, PubMed:9872744). Within the heterodimeric GABA receptor, only GABBR1 seems to bind agonists, while GABBR2 mediates coupling to G proteins (PubMed:18165688). Ligand binding causes a conformation change that triggers signaling via guanine nucleotide-binding proteins (G proteins) and modulates the activity of down-stream effectors, such as adenylate cyclase (PubMed:10075644, PubMed:10773016, PubMed:10906333, PubMed:24305054, PubMed:9872744). Signaling inhibits adenylate cyclase, stimulates…
Heterodimer of GABBR1 and GABBR2 (PubMed:10773016, PubMed:15617512, PubMed:18165688, PubMed:22660477, PubMed:24305054, PubMed:9872316, PubMed:9872744). Homodimers may form, but are inactive (PubMed:15617512, PubMed:9872316). Isoform 1E (without C-terminal intracellular domain) is unable to dimerize via a coiled-coil interaction with GABBR2 (PubMed:10906333). Interacts (via C-terminus) with ATF4…
Cell membrane, Postsynaptic cell membrane, Cell projection, dendrite, Secreted
Compare the prediction with experimentally determined structures of the same protein:
| PDB ID | Method | Resolution | Chains and residues |
|---|---|---|---|
| 4PAS | X-ray | 1.62 Å | A=879-919 |
| 4MS4 | X-ray | 1.9 Å | A=165-576 |
| 4MR7 | X-ray | 2.15 Å | A=165-576 |
| 4MR8 | X-ray | 2.15 Å | A=165-576 |
| 4MQF | X-ray | 2.22 Å | A=165-576 |
| 4MS1 | X-ray | 2.25 Å | A=165-576 |
| 4MQE | X-ray | 2.35 Å | A=165-576 |
| 4MR9 | X-ray | 2.35 Å | A=165-576 |
| 4MS3 | X-ray | 2.5 Å | A=165-576 |
| 4MRM | X-ray | 2.86 Å | A=165-576 |
| 7C7S | EM | 2.9 Å | A=15-919 |
| 7C7Q | EM | 3.0 Å | A=15-862 |
| 6W2Y | EM | 3.2 Å | A/B=153-961 |
| 6WIV | EM | 3.3 Å | A=153-919 |
| 7EB2 | EM | 3.5 Å | C=15-919 |
| 7CUM | EM | 3.52 Å | A=165-900 |
| 6W2X | EM | 3.6 Å | A=153-961 |
| 6UO8 | EM | 3.63 Å | A=165-919 |
| 6VJM | EM | 3.97 Å | A=165-919 |
| 7CA3 | EM | 4.5 Å | A=165-900 |
Showing 20 of 24 experimental structures (best resolution first).
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