Proprotein convertase subtilisin/kexin type 9 (PCSK9) is a 692-residue protein from Homo sapiens. This is its AlphaFold structure prediction, created 1 Aug 2025. UniProt accession: Q8NBP7.
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The mean pLDDT of this model is 85.2 (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 | 67% |
| 70 to 90 | Confident: backbone generally right | 15% |
| 50 to 70 | Low: treat with caution | 5% |
| Below 50 | Very low: often disordered regions | 14% |
What pLDDT means and how to read it
Crucial player in the regulation of plasma cholesterol homeostasis. Binds to low-density lipid receptor family members: low density lipoprotein receptor (LDLR), very low density lipoprotein receptor (VLDLR), apolipoprotein E receptor (LRP1/APOER) and apolipoprotein receptor 2 (LRP8/APOER2), and promotes their degradation in intracellular acidic compartments (PubMed:18039658). Acts via a non-proteolytic mechanism to enhance the degradation of the hepatic LDLR through a clathrin LDLRAP1/ARH-mediated pathway. May prevent the recycling of LDLR from endosomes to the cell surface or direct it to lysosomes for degradation. Can induce ubiquitination of LDLR leading to its subsequent degradation…
Monomer. Can self-associate to form dimers and higher multimers which may have increased LDLR degrading activity. The precursor protein but not the mature protein may form multimers. Interacts with APOB, VLDLR, LRP8/APOER2 and BACE1. The full-length immature form (pro-PCSK9) interacts with SCNN1A, SCNN1B and SCNN1G. The pro-PCSK9 form (via C-terminal domain) interacts with LDLR. Interacts (via…
Cytoplasm, Secreted, Endosome, Lysosome, Cell surface, Endoplasmic reticulum, Golgi apparatus
Compare the prediction with experimentally determined structures of the same protein:
| PDB ID | Method | Resolution | Chains and residues |
|---|---|---|---|
| 7S5H | X-ray | 1.27 Å | A=31-152, B=153-452 |
| 6XIC | X-ray | 1.38 Å | A=32-152, B=153-452 |
| 6XIE | X-ray | 1.43 Å | A=31-152, B=153-452 |
| 6XID | X-ray | 1.48 Å | A=31-152, B=153-452 |
| 6U26 | X-ray | 1.53 Å | A/B=31-692 |
| 6XIB | X-ray | 1.55 Å | A=31-152, B=153-452 |
| 6XIF | X-ray | 1.77 Å | A=31-152, B=153-452 |
| 4NMX | X-ray | 1.85 Å | A=31-152, B=153-452 |
| 2QTW | X-ray | 1.9 Å | A=29-152, B=153-692 |
| 8WFR | X-ray | 1.95 Å | A=31-152, B=153-692 |
| 8FVL | X-ray | 1.96 Å | A=1-152, B=153-692 |
| 8VDV | X-ray | 1.97 Å | A=61-152, B=153-681 |
| 2P4E | X-ray | 1.98 Å | A/P=1-692 |
| 6U2P | X-ray | 2.04 Å | A/B=31-692 |
| 7S5G | X-ray | 2.04 Å | A=31-152, B=153-452 |
| 6MV5 | X-ray | 2.1 Å | P=32-53 |
| 6U2N | X-ray | 2.15 Å | A/B=31-692 |
| 5VLK | X-ray | 2.2 Å | A=1-452 |
| 6E4Z | X-ray | 2.2 Å | P=32-53 |
| 7ANQ | X-ray | 2.2 Å | A=452-682 |
Showing 20 of 62 experimental structures (best resolution first).
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