Sodium/potassium-transporting ATPase subunit alpha-1 (ATP1A1) is a 1021-residue protein from Sus scrofa. This is its AlphaFold structure prediction, created 1 Aug 2025. UniProt accession: P05024.
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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 | 64% |
| 70 to 90 | Confident: backbone generally right | 30% |
| 50 to 70 | Low: treat with caution | 3% |
| Below 50 | Very low: often disordered regions | 3% |
What pLDDT means and how to read it
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. It undergoes ATP-driven conformational changes that allow alternating binding and release of Na(+) and K(+) ions across the membrane (By similarity). This process maintains essential Na(+) and K(+) gradients for membrane potential and cellular function. Could also be part of an osmosensory signaling pathway that senses body-fluid sodium levels and controls salt intake behavior as well as voluntary water intake to regulate sodium homeostasis (By similarity)
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. The particular alpha/beta/FXYD combination in each…
Cell membrane, Basolateral cell membrane, Cell membrane, sarcolemma, Cell projection, axon, Melanosome
Compare the prediction with experimentally determined structures of the same protein:
| PDB ID | Method | Resolution | Chains and residues |
|---|---|---|---|
| 3WGU | X-ray | 2.8 Å | A/C=6-1021 |
| 3WGV | X-ray | 2.8 Å | A/C=6-1021 |
| 8JBK | X-ray | 2.8 Å | A/C=1-1021 |
| 7WYT | X-ray | 2.9 Å | A/C=6-1021 |
| 8JBM | X-ray | 2.9 Å | A/C=1-1021 |
| 8JBL | X-ray | 3.0 Å | A/C=1-1021 |
| 7DDL | X-ray | 3.2 Å | A/C=6-1021 |
| 7D91 | X-ray | 3.35 Å | A=6-1021 |
| 4HYT | X-ray | 3.4 Å | A/C=1-1021 |
| 4RES | X-ray | 3.41 Å | A/C=1-1021 |
| 7DDH | X-ray | 3.46 Å | A/C=6-1021 |
| 3B8E | X-ray | 3.5 Å | A/C=24-1021 |
| 3KDP | X-ray | 3.5 Å | A/C=24-1021 |
| 7D94 | X-ray | 3.5 Å | A/C=6-1021 |
| 7DDK | X-ray | 3.5 Å | A/C=6-1021 |
| 7D93 | X-ray | 3.65 Å | A/C=6-1021 |
| 7WYS | X-ray | 3.71 Å | A/C=6-1021 |
| 7DDI | X-ray | 3.72 Å | A/C=6-1021 |
| 7D92 | X-ray | 3.9 Å | A=6-1021 |
| 4RET | X-ray | 4.0 Å | A/C=1-1021 |
Showing 20 of 26 experimental structures (best resolution first).
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