E3 ubiquitin-protein ligase MYLIP (MYLIP) is a 445-residue protein from Homo sapiens. This is its AlphaFold structure prediction, created 1 Aug 2025. UniProt accession: Q8WY64.
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The mean pLDDT of this model is 85.8 (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 | 62% |
| 70 to 90 | Confident: backbone generally right | 24% |
| 50 to 70 | Low: treat with caution | 8% |
| Below 50 | Very low: often disordered regions | 7% |
What pLDDT means and how to read it
E3 ubiquitin-protein ligase that mediates ubiquitination and subsequent proteasomal degradation of myosin regulatory light chain (MRLC), LDLR, VLDLR and LRP8. Activity depends on E2 enzymes of the UBE2D family. Proteasomal degradation of MRLC leads to inhibit neurite outgrowth in presence of NGF by counteracting the stabilization of MRLC by saposin-like protein (CNPY2/MSAP) and reducing CNPY2-stimulated neurite outgrowth. Acts as a sterol-dependent inhibitor of cellular cholesterol uptake by mediating ubiquitination and subsequent degradation of LDLR
Homodimer. Interacts with the E2 ubiquitin-conjugating enzyme, UBE2D1 (via RING-type zinc finger). Interacts with myosin regulatory light chain (MRLC) and TMEM4
Cytoplasm, Cell membrane
Compare the prediction with experimentally determined structures of the same protein:
| PDB ID | Method | Resolution | Chains and residues |
|---|---|---|---|
| 9SA1 | X-ray | 1.06 Å | A/B=369-445 |
| 9SA2 | X-ray | 1.1 Å | A/B/C/D=369-445 |
| 13SY | X-ray | 1.29 Å | A/B/C/D=369-445 |
| 13SQ | X-ray | 1.3 Å | A/B/C/D=369-445 |
| 13SL | X-ray | 1.34 Å | A/B/C/D=369-445 |
| 13SX | X-ray | 1.36 Å | A/B/C/D=369-445 |
| 13ST | X-ray | 1.37 Å | A/B/C/D=369-445 |
| 13SW | X-ray | 1.37 Å | A/B/C/D=369-445 |
| 13SM | X-ray | 1.4 Å | A/B/C/D=369-445 |
| 13SE | X-ray | 1.44 Å | A/B/C/D=369-445 |
| 13SN | X-ray | 1.44 Å | A/B/C/D=369-445 |
| 13SJ | X-ray | 1.47 Å | A/B/C/D=369-445 |
| 13SB | X-ray | 1.48 Å | A/B/C/D=369-445 |
| 13SC | X-ray | 1.48 Å | A/B/C/D=369-445 |
| 13SZ | X-ray | 1.49 Å | A/B/C/D=369-445 |
| 13SU | X-ray | 1.5 Å | A/B/C/D=369-445 |
| 13TA | X-ray | 1.51 Å | A/B/C/D=369-445 |
| 13SD | X-ray | 1.52 Å | A/B/C/D=369-445 |
| 13SI | X-ray | 1.54 Å | A/B/C/D=369-445 |
| 13SK | X-ray | 1.54 Å | A/B/C/D=369-445 |
Showing 20 of 35 experimental structures (best resolution first).
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