Very low-density lipoprotein receptor (VLDLR) is a 873-residue protein from Homo sapiens. This is its AlphaFold structure prediction, created 1 Aug 2025. UniProt accession: P98155.
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The mean pLDDT of this model is 75.7 (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 | 25% |
| 70 to 90 | Confident: backbone generally right | 51% |
| 50 to 70 | Low: treat with caution | 10% |
| Below 50 | Very low: often disordered regions | 15% |
What pLDDT means and how to read it
Multifunctional cell surface receptor that binds VLDL and transports it into cells by endocytosis and therefore plays an important role in energy metabolism. Also binds to a wide range of other molecules including Reelin/RELN or apolipoprotein E/APOE-containing ligands as well as clusterin/CLU (PubMed:24381170, PubMed:30873003). In the off-state of the pathway, forms homooligomers or heterooligomers with LRP8 (PubMed:30873003). Upon binding to ligands, homooligomers are rearranged to higher order receptor clusters that transmit the extracellular RELN signal to intracellular signaling processes by binding to DAB1 (PubMed:30873003). This interaction results in phosphorylation of DAB1 leading…
Homooligomer (PubMed:30873003). Binds to the extracellular matrix protein Reelin/RELN (PubMed:30873003). Interacts with LRP8 (PubMed:30873003). Interacts with LDLRAP1 (By similarity). Interacts with SNX17 (By similarity). Interacts with DAB1. Interacts with PCSK9. Interacts with PAFAH1B3 and PAFAH1B2, the catalytic complex of (PAF-AH (I)) heterotetrameric enzyme; these interactions may modulate…
Cell membrane, Membrane, clathrin-coated pit
Compare the prediction with experimentally determined structures of the same protein:
| PDB ID | Method | Resolution | Chains and residues |
|---|---|---|---|
| 9DQZ | EM | 2.9 Å | M/N/O/P=33-110 |
| 8IHP | EM | 3.0 Å | M/N/O=111-149 |
| 9UIO | EM | 3.03 Å | R/S/T=32-110 |
| 9EAU | EM | 3.06 Å | Y/Z=111-149 |
| 8UFC | EM | 3.09 Å | V/W/X/Y=31-108 |
| 9WSL | EM | 3.27 Å | R/S/T=32-110 |
| 8XI4 | EM | 3.4 Å | M/N/O/P=31-113 |
| 8XI5 | EM | 3.4 Å | M/N/O/P=191-231, Q/R/S/T=111-151 |
| 8YW1 | EM | 3.44 Å | C=111-231 |
| 8YVZ | EM | 3.45 Å | E/R/S/T=110-151 |
| 3DPR | X-ray | 3.5 Å | E=113-151 |
| 8X0K | EM | 3.5 Å | D/H/L/P=113-149 |
| 8X0L | EM | 3.5 Å | D/H/L=113-149 |
| 8X0M | EM | 3.5 Å | D/H=113-149 |
| 8YW0 | EM | 3.55 Å | E/R/T=191-230 |
| 8UA4 | EM | 3.58 Å | R=33-68 |
| 1V9U | X-ray | 3.6 Å | 5=111-151 |
| 9L99 | EM | 3.6 Å | N=31-110 |
| 8UA8 | EM | 3.7 Å | R=72-108 |
| 8YW2 | EM | 3.7 Å | A=70-231 |
Showing 20 of 27 experimental structures (best resolution first).
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