Sodium/potassium-transporting ATPase subunit beta-1 (ATP1B1) is a 303-residue protein from Sus scrofa. This is its AlphaFold structure prediction, created 1 Aug 2025. UniProt accession: P05027.
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The mean pLDDT of this model is 88.9 (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 | 74% |
| 70 to 90 | Confident: backbone generally right | 19% |
| 50 to 70 | Low: treat with caution | 6% |
| Below 50 | Very low: often disordered regions | 2% |
What pLDDT means and how to read it
Non-catalytic subunit of the Na(+)/K(+)-ATPase pump that hydrolyzes ATP to exchange ions across the plasma membrane, exporting 3 Na(+) and importing 2 K(+) per cycle against electrochemical gradients. The beta subunit is important for the folding, stability, and targeting of the Na(+)/K(+)-ATPase pump to the plasma membranes (By similarity). In addition, acts as a homotypic cell adhesion molecule in epithelia cells. Interactions between ATP1B1 on neighboring cells are critical for proper lateral polarization of the Na(+)/K(+)-ATPase pump and for stabilizing cell-cell adhesion (By similarity). Plays a role in innate immunity by enhancing virus-triggered induction of interferons (IFNs) and…
The sodium/potassium-transporting ATPase is composed of a catalytic alpha subunit, an auxiliary non-catalytic beta subunit and an additional regulatory subunit, called FXYD. There are four, three and seven isoforms for the alpha, beta and regulatory subunits, respectively, among which the expression of the alpha isoforms is tissue-specific. Interacts with catalytic subunit ATP12A (By…
Cell membrane, Apical cell membrane, Cell membrane, sarcolemma
Compare the prediction with experimentally determined structures of the same protein:
| PDB ID | Method | Resolution | Chains and residues |
|---|---|---|---|
| 3WGU | X-ray | 2.8 Å | B/D=1-303 |
| 3WGV | X-ray | 2.8 Å | B/D=1-303 |
| 8JBK | X-ray | 2.8 Å | B/D=1-303 |
| 7WYT | X-ray | 2.9 Å | B/D=1-303 |
| 8JBM | X-ray | 2.9 Å | B/D=1-303 |
| 8JBL | X-ray | 3.0 Å | B/D=1-303 |
| 7DDL | X-ray | 3.2 Å | B/D=1-303 |
| 7D91 | X-ray | 3.35 Å | B=1-303 |
| 4HYT | X-ray | 3.4 Å | B/D=1-303 |
| 4RES | X-ray | 3.41 Å | B/D=1-303 |
| 7DDH | X-ray | 3.46 Å | B/D=1-303 |
| 3B8E | X-ray | 3.5 Å | B/D=28-73 |
| 3KDP | X-ray | 3.5 Å | B/D=18-303 |
| 7D94 | X-ray | 3.5 Å | B/D=1-303 |
| 7DDK | X-ray | 3.5 Å | B/D=1-303 |
| 7D93 | X-ray | 3.65 Å | B/D=1-303 |
| 7WYS | X-ray | 3.71 Å | B/D=1-303 |
| 7DDI | X-ray | 3.72 Å | B/D=1-303 |
| 9VJ2 | X-ray | 3.79 Å | B=1-303 |
| 7D92 | X-ray | 3.9 Å | B=1-303 |
Showing 20 of 27 experimental structures (best resolution first).
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