von Hippel-Lindau disease tumor suppressor (VHL) is a 213-residue protein from Homo sapiens. This is its AlphaFold structure prediction, created 1 Aug 2025. UniProt accession: P40337.
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The mean pLDDT of this model is 84.4 (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 | 70% |
| 70 to 90 | Confident: backbone generally right | 3% |
| 50 to 70 | Low: treat with caution | 14% |
| Below 50 | Very low: often disordered regions | 13% |
What pLDDT means and how to read it
Involved in the ubiquitination and subsequent proteasomal degradation via the von Hippel-Lindau ubiquitination complex (PubMed:10944113, PubMed:17981124, PubMed:19584355). Seems to act as a target recruitment subunit in the E3 ubiquitin ligase complex and recruits hydroxylated hypoxia-inducible factor (HIF) under normoxic conditions (PubMed:10944113, PubMed:17981124). Involved in transcriptional repression through interaction with HIF1A, HIF1AN and histone deacetylases (PubMed:10944113, PubMed:17981124). Ubiquitinates, in an oxygen-responsive manner, ADRB2 (PubMed:19584355). Acts as a negative regulator of mTORC1 by promoting ubiquitination and degradation of RPTOR (PubMed:34290272)
Component of the VCB (VHL-Elongin BC-CUL2) complex; this complex acts as a ubiquitin-ligase E3 and directs proteasome-dependent degradation of targeted proteins. Interacts with CUL2; this interaction is dependent on the integrity of the trimeric VCB complex. Interacts (via the beta domain) with HIF1A (via the NTAD domain); this interaction mediates degradation of HIF1A in normoxia and, in…
Cytoplasm, Cell membrane, Endoplasmic reticulum, Nucleus
Compare the prediction with experimentally determined structures of the same protein:
| PDB ID | Method | Resolution | Chains and residues |
|---|---|---|---|
| 7Z76 | X-ray | 1.32 Å | C=54-213 |
| 9GIO | X-ray | 1.49 Å | C=54-213 |
| 7JTO | X-ray | 1.7 Å | L=54-213 |
| 8BDS | X-ray | 1.72 Å | C=54-213 |
| 4AJY | X-ray | 1.73 Å | V=54-213 |
| 6GMR | X-ray | 1.75 Å | V=54-213 |
| 6HR2 | X-ray | 1.76 Å | B/F=61-209 |
| 6I7Q | X-ray | 1.8 Å | V=54-213 |
| 8BB3 | X-ray | 1.8 Å | L=54-213 |
| 6GFX | X-ray | 1.83 Å | C=54-213 |
| 1LM8 | X-ray | 1.85 Å | V=54-213 |
| 6ZHC | X-ray | 1.92 Å | AAA=59-213 |
| 6GMN | X-ray | 1.94 Å | C/F/I/L=54-213 |
| 6I7R | X-ray | 1.95 Å | V=54-213 |
| 7Z77 | X-ray | 1.97 Å | C=54-213 |
| 8P0F | X-ray | 1.98 Å | A/D=54-213 |
| 9BOL | X-ray | 1.99 Å | C/F=54-213 |
| 1LQB | X-ray | 2.0 Å | C=54-213 |
| 4B9K | X-ray | 2.0 Å | C/F/I/L=54-213 |
| 6BVB | X-ray | 2.0 Å | V=54-213 |
Showing 20 of 142 experimental structures (best resolution first).
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