Beta-arrestin-1 (ARRB1) is a 418-residue protein from Homo sapiens. This is its AlphaFold structure prediction, created 1 Aug 2025. UniProt accession: P49407.
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The mean pLDDT of this model is 82.2 (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 | 26% |
| 50 to 70 | Low: treat with caution | 8% |
| Below 50 | Very low: often disordered regions | 12% |
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, PubMed:40384633). 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…
Monomer. Homodimer. Homooligomer; the self-association is mediated by InsP6-binding. Heterooligomer with ARRB2; the association is mediated by InsP6-binding. Interacts with GPR143. 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…
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 |
|---|---|---|---|
| 8AS4 | X-ray | 2.3 Å | A/B=1-418 |
| 8ZYT | EM | 2.65 Å | B=2-382 |
| 8ZYU | EM | 2.65 Å | B=2-382 |
| 2IV8 | X-ray | 2.8 Å | P/Q=383-402 |
| 8ZYY | EM | 2.83 Å | B=2-382 |
| 9UYN | EM | 2.9 Å | A=1-376 |
| 9LXR | EM | 3.07 Å | B=4-376 |
| 9LY2 | EM | 3.1 Å | B=4-393 |
| 9MBA | EM | 3.14 Å | B/C=1-376 |
| 8AS2 | X-ray | 3.2 Å | A=1-359 |
| 9LXP | EM | 3.2 Å | B=4-376 |
| 9UYI | EM | 3.2 Å | A=1-376 |
| 9L8L | EM | 3.22 Å | C=2-393 |
| 6TKO | EM | 3.3 Å | B=1-418 |
| 7SRS | EM | 3.3 Å | C=2-376 |
| 8JRV | EM | 3.3 Å | A/H/L=1-379 |
| 9UYH | EM | 3.3 Å | A=1-376 |
| 9UYJ | EM | 3.3 Å | A=1-376 |
| 9UYL | EM | 3.3 Å | A=1-376 |
| 9LY3 | EM | 3.4 Å | B=4-393 |
Showing 20 of 32 experimental structures (best resolution first).
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