Gamma-aminobutyric acid type B receptor subunit 2 (GABBR2) is a 941-residue protein from Homo sapiens. This is its AlphaFold structure prediction, created 1 Aug 2025. UniProt accession: O75899.
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The mean pLDDT of this model is 77.8 (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 | 46% |
| 70 to 90 | Confident: backbone generally right | 28% |
| 50 to 70 | Low: treat with caution | 5% |
| Below 50 | Very low: often disordered regions | 20% |
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: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:24305054). Signaling inhibits adenylate cyclase, stimulates phospholipase A2, activates potassium channels, inactivates…
Heterodimer of GABBR1 and GABBR2 (PubMed:10773016, PubMed:10906333, PubMed:15617512, PubMed:18165688, PubMed:22660477, PubMed:24305054, PubMed:9872316, PubMed:9872744). Homodimers may form, but are inactive (PubMed:15617512). Interacts (via C-terminus) with ATF4 (via leucine zipper domain) (By similarity)
Cell membrane, Postsynaptic cell membrane
Compare the prediction with experimentally determined structures of the same protein:
| PDB ID | Method | Resolution | Chains and residues |
|---|---|---|---|
| 4PAS | X-ray | 1.62 Å | B=779-819 |
| 4MS4 | X-ray | 1.9 Å | B=42-466 |
| 4MR7 | X-ray | 2.15 Å | B=42-466 |
| 4MR8 | X-ray | 2.15 Å | B=42-466 |
| 4MQF | X-ray | 2.22 Å | B=42-466 |
| 4MS1 | X-ray | 2.25 Å | B=42-466 |
| 4MQE | X-ray | 2.35 Å | B=42-466 |
| 4MR9 | X-ray | 2.35 Å | B=42-466 |
| 6OCP | X-ray | 2.35 Å | P/Q/R=895-909 |
| 4F11 | X-ray | 2.38 Å | A=42-466 |
| 4MS3 | X-ray | 2.5 Å | B=42-466 |
| 4MRM | X-ray | 2.86 Å | B=42-466 |
| 7C7S | EM | 2.9 Å | B=41-819 |
| 7C7Q | EM | 3.0 Å | B=41-780 |
| 4F12 | X-ray | 3.02 Å | A=42-466 |
| 6M8R | X-ray | 3.2 Å | K/L=876-913 |
| 6WIV | EM | 3.3 Å | B=1-819 |
| 7EB2 | EM | 3.5 Å | D=41-819 |
| 7CUM | EM | 3.52 Å | B=1-787 |
| 6W2X | EM | 3.6 Å | B=42-941 |
Showing 20 of 26 experimental structures (best resolution first).
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