Beta-arrestin-1 (Arrb1) is a 418-residue protein from Rattus norvegicus. This is its AlphaFold structure prediction, created 1 Aug 2025. UniProt accession: P29066.
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The mean pLDDT of this model is 82.5 (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 band | Meaning | Share of residues |
|---|---|---|
| Above 90 | Very high: backbone and side chains are usually accurate | 57% |
| 70 to 90 | Confident: backbone generally right | 23% |
| 50 to 70 | Low: treat with caution | 8% |
| Below 50 | Very low: often disordered regions | 11% |
What pLDDT means and how to read it
Functions in regulating agonist-mediated G protein-coupled receptor (GPCR) signaling by mediating both receptor desensitization and resensitization processes (PubMed:37209686, PubMed:38175886). During homologous desensitization, beta-arrestins bind to the GPCR-phosphorylated receptor and sterically preclude its coupling to the cognate G protein; the binding appears to require additional receptor determinants exposed only in the active receptor conformation. The beta-arrestins target many receptors for internalization by acting as endocytic adapters (CLASPs, clathrin-associated sorting proteins) and recruiting the GPRCs to the adapter protein 2 complex 2 (AP-2) in clathrin-coated pits…
Monomer. Homodimer. Homooligomer; the self-association is mediated by InsP6-binding. Heterooligomer with ARRB2; the association is mediated by InsP6-binding. Interacts with ADRB2 (phosphorylated). Interacts with CHRM2 (phosphorylated). Interacts with LHCGR. Interacts with CYTH2 and CASR. Interacts with AP2B1 (dephosphorylated at 'Tyr-737'); phosphorylation of AP2B1 at 'Tyr-737' disrupts the…
Cytoplasm, Nucleus, Cell membrane, Membrane, clathrin-coated pit, Cell projection, pseudopodium, Cytoplasmic vesicle
Compare the prediction with experimentally determined structures of the same protein:
| PDB ID | Method | Resolution | Chains and residues |
|---|---|---|---|
| 4JQI | X-ray | 2.6 Å | A=2-393 |
| 8HST | X-ray | 2.66 Å | A/B=1-394 |
| 9KYU | EM | 2.72 Å | A/D=1-418 |
| 6KL7 | X-ray | 2.79 Å | A/B=1-418 |
| 8HSV | X-ray | 3.0 Å | A/B=1-394 |
| 8I0N | EM | 3.26 Å | A/B=1-418 |
| 9BT8 | EM | 3.34 Å | B=2-393 |
| 9CX9 | EM | 3.34 Å | A=2-393 |
| 8J8Z | EM | 3.4 Å | A/B=1-418 |
| 8GO8 | EM | 3.41 Å | A/B=1-418 |
| 9CX3 | EM | 3.47 Å | B=2-393 |
| 9DNM | EM | 3.47 Å | A=2-393 |
| 9DNG | EM | 3.52 Å | A=2-393 |
| 8JA3 | EM | 3.94 Å | A/B=1-357 |
| 6U1N | EM | 4.0 Å | C=2-393 |
| 8I0Q | EM | 4.45 Å | A/B=1-418 |
| 8GP3 | EM | 4.8 Å | A/B=1-418 |
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