Sarcoplasmic/endoplasmic reticulum calcium ATPase 1 (ATP2A1) is a 1001-residue protein from Oryctolagus cuniculus. This is its AlphaFold structure prediction, created 1 Aug 2025. UniProt accession: P04191.
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The mean pLDDT of this model is 86.8 (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 | 46% |
| 70 to 90 | Confident: backbone generally right | 48% |
| 50 to 70 | Low: treat with caution | 6% |
| Below 50 | Very low: often disordered regions | 1% |
What pLDDT means and how to read it
Key regulator of striated muscle performance by acting as the major Ca(2+) ATPase responsible for the reuptake of cytosolic Ca(2+) into the sarcoplasmic reticulum. Catalyzes the hydrolysis of ATP coupled with the translocation of calcium from the cytosol to the sarcoplasmic reticulum lumen (PubMed:10914677, PubMed:11438520, PubMed:15189864, PubMed:18075584, PubMed:23996003, PubMed:24270570, PubMed:29081402). Contributes to calcium sequestration involved in muscular excitation/contraction
Interacts with sarcolipin (SLN) (PubMed:23455422, PubMed:23455424, PubMed:29081402). Interacts with phospholamban (PLN) (PubMed:10551848, PubMed:23996003, PubMed:29081402, PubMed:8428955). Interacts with myoregulin (MRLN) (By similarity). Interacts with DWORF (By similarity). Interacts with VMP1 (By similarity)
Endoplasmic reticulum membrane, Sarcoplasmic reticulum membrane
Compare the prediction with experimentally determined structures of the same protein:
| PDB ID | Method | Resolution | Chains and residues |
|---|---|---|---|
| 3AR4 | X-ray | 2.15 Å | A=1-993 |
| 3AR7 | X-ray | 2.15 Å | A=1-993 |
| 3AR5 | X-ray | 2.2 Å | A=1-993 |
| 3AR6 | X-ray | 2.2 Å | A=1-993 |
| 3N5K | X-ray | 2.2 Å | A/B=1-993 |
| 1WPG | X-ray | 2.3 Å | A/B/C/D=1-993 |
| 3AR3 | X-ray | 2.3 Å | A=1-993 |
| 1SU4 | X-ray | 2.4 Å | A=1-993 |
| 2AGV | X-ray | 2.4 Å | A/B=1-993 |
| 2ZBD | X-ray | 2.4 Å | A=1-993 |
| 2ZBF | X-ray | 2.4 Å | A=1-993 |
| 3W5D | X-ray | 2.45 Å | A=1-993 |
| 2DQS | X-ray | 2.5 Å | A=1-993 |
| 3AR2 | X-ray | 2.5 Å | A=1-993 |
| 3FGO | X-ray | 2.5 Å | A/B=1-993 |
| 3W5C | X-ray | 2.5 Å | A=1-993 |
| 4BEW | X-ray | 2.5 Å | A/B=1-994 |
| 4UU0 | X-ray | 2.5 Å | A=1-993 |
| 5ZMW | X-ray | 2.5 Å | A=1-993 |
| 2ZBG | X-ray | 2.55 Å | A=1-993 |
Showing 20 of 76 experimental structures (best resolution first).
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