Beta-arrestin-1 (ARRB1) is a 418-residue protein from Bos taurus. This is its AlphaFold structure prediction, created 1 Aug 2025. UniProt accession: P17870.
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The mean pLDDT of this model is 82.6 (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 | 58% |
| 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. 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 (CCPs). However, the extent of…
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 |
|---|---|---|---|
| 1G4M | X-ray | 1.9 Å | A/B=1-393 |
| 1G4R | X-ray | 2.2 Å | A=1-393 |
| 3GC3 | X-ray | 2.2 Å | A=1-393 |
| 7DFC | X-ray | 2.49 Å | A=1-418 |
| 7DFA | X-ray | 2.54 Å | A=1-418 |
| 9WSV | EM | 2.8 Å | C=1-393 |
| 9WSX | EM | 2.8 Å | C=1-393 |
| 1JSY | X-ray | 2.9 Å | A=1-418 |
| 1ZSH | X-ray | 2.9 Å | A=1-418 |
| 2WTR | X-ray | 2.9 Å | A/B=1-418 |
| 8TII | EM | 3.0 Å | A=1-418 |
| 9LZ2 | EM | 3.0 Å | A=1-393 |
| 8JAF | EM | 3.1 Å | A=5-362 |
| 7DF9 | X-ray | 3.17 Å | A=1-418 |
| 8J97 | EM | 3.2 Å | A=5-357 |
| 8WU1 | EM | 3.2 Å | C=1-393 |
| 9LZ1 | EM | 3.2 Å | A=1-393 |
| 7DFB | X-ray | 3.28 Å | A=1-418 |
| 9E82 | EM | 3.4 Å | A=1-418 |
| 3GD1 | X-ray | 3.5 Å | C/E=1-393 |
Showing 20 of 23 experimental structures (best resolution first).
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