Beta-2 adrenergic receptor (ADRB2) is a 413-residue protein from Homo sapiens. This is its AlphaFold structure prediction, created 1 Aug 2025. UniProt accession: P07550.
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The mean pLDDT of this model is 79.1 (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 | 60% |
| 70 to 90 | Confident: backbone generally right | 10% |
| 50 to 70 | Low: treat with caution | 9% |
| Below 50 | Very low: often disordered regions | 21% |
What pLDDT means and how to read it
G protein-coupled receptor for catecholamines that couples to both G(s) and G(i) proteins, activating bifurcated signaling pathways (PubMed:2831218, PubMed:7915137). ADRB2 binds epinephrine (Epi) with an approximately 30-fold greater affinity than norepinephrine (NE) (PubMed:2831218, PubMed:33093660, PubMed:7915137). In the heart, Epi- and NE-activated ADRB2 induces rapid and slow cardiomyocyte contraction rate, respectively (By similarity). Both NE and Epi promote coupling to G(s)/PKA pathway to regulate myocyte contraction rate (By similarity). Epi also promotes ADRB2 coupling to G(i) proteins to exert cardioprotective effects especially in the conditions of hypoxia and oxidative stress…
Binds NHERF1 and GPRASP1 (PubMed:9560162). Interacts with ARRB1 and ARRB2. Interacts with SRC (PubMed:9924018). Interacts with USP20 and USP33 (PubMed:19424180, PubMed:23166351). Interacts with VHL; the interaction, which is increased on hydroxylation of ADRB2, ubiquitinates ADRB2 leading to its degradation. Interacts with EGLN3; the interaction hydroxylates ADRB2 facilitating VHL-E3…
Cell membrane, Golgi apparatus
Compare the prediction with experimentally determined structures of the same protein:
| PDB ID | Method | Resolution | Chains and residues |
|---|---|---|---|
| 1GQ4 | X-ray | 1.9 Å | A=336-366 |
| 2RH1 | X-ray | 2.4 Å | A=1-230, A=264-365 |
| 6PS2 | X-ray | 2.4 Å | A=1-230, A=264-348 |
| 9RKF | X-ray | 2.45 Å | A=28-230, A=264-342 |
| 9RKG | X-ray | 2.45 Å | A=29-230, A=264-342 |
| 5D5A | X-ray | 2.48 Å | A=1-230, A=264-365 |
| 6PS3 | X-ray | 2.5 Å | A=1-230, A=264-348 |
| 9RKH | X-ray | 2.5 Å | A=29-230, A=264-342 |
| 6PS4 | X-ray | 2.6 Å | A=1-230, A=264-348 |
| 9RKI | X-ray | 2.6 Å | A=29-230, A=264-342 |
| 9U4Y | EM | 2.67 Å | R=1-30, R=41-326 |
| 5X7D | X-ray | 2.7 Å | A=1-230, A=264-365 |
| 6PS6 | X-ray | 2.7 Å | A=1-230, A=264-348 |
| 9I54 | EM | 2.72 Å | R=1-30 |
| 4LDE | X-ray | 2.79 Å | A=29-348 |
| 3D4S | X-ray | 2.8 Å | A=1-230, A=264-348 |
| 6PRZ | X-ray | 2.8 Å | A=1-230, A=264-348 |
| 9I52 | EM | 2.8 Å | R=1-30 |
| 3NY8 | X-ray | 2.84 Å | A=1-230, A=264-348 |
| 3NY9 | X-ray | 2.84 Å | A=1-230, A=264-348 |
Showing 20 of 145 experimental structures (best resolution first).
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