Melanocyte protein PMEL (PMEL) is a 661-residue protein from Homo sapiens. This is its AlphaFold structure prediction, created 1 Aug 2025. UniProt accession: P40967.
Explore in 3D Color by confidence AlphaFold DB UniProt
The mean pLDDT of this model is 68.4 (low 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 | 34% |
| 70 to 90 | Confident: backbone generally right | 21% |
| 50 to 70 | Low: treat with caution | 10% |
| Below 50 | Very low: often disordered regions | 35% |
What pLDDT means and how to read it
Forms physiological amyloids that play a central role in melanosome morphogenesis and pigmentation. The maturation of unpigmented premelanosomes from stage I to II is marked by assembly of processed amyloidogenic fragments into parallel fibrillar sheets, which elongate the vesicle into a striated ellipsoidal shape. In pigmented stage III and IV melanosomes, the amyloid matrix serves as a platform where eumelanin precursors accumulate at high local concentrations for pigment formation. May prevent pigmentation-associated toxicity by sequestering toxic reaction intermediates of eumelanin biosynthesis pathway
Homodimer; disulfide-linked. Dimerization in the endoplasmic reticulum and early Golgi prevents premature fibril formation. The dimers are resolved to monomers in late- or post-Golgi compartments (PubMed:26694611). Heterooligomer; amyloid-type. Processed amyloidogenic fragments assemble into fibrils that further organize into beta-sheet quaternary amyloid structures (PubMed:28272432,…
Endoplasmic reticulum membrane, Golgi apparatus, cis-Golgi network membrane, Endosome, multivesicular body, Melanosome, Extracellular vesicle, Secreted
Compare the prediction with experimentally determined structures of the same protein:
| PDB ID | Method | Resolution | Chains and residues |
|---|---|---|---|
| 5EU5 | X-ray | 1.54 Å | C=280-288 |
| 9JST | EM | 1.79 Å | A/B/C/D/E/F/G/H=148-182 |
| 9JSU | EM | 1.79 Å | A/B/C/D/E/F/G/H=151-183 |
| 9JSV | EM | 1.79 Å | A/B/C/D/E/F/G/H=149-182 |
| 9JSX | EM | 1.79 Å | A/B/C/D/E/F/G/H=149-182 |
| 1TVB | X-ray | 1.8 Å | C/F=209-217 |
| 1TVH | X-ray | 1.8 Å | C/F=209-217 |
| 3CC5 | X-ray | 1.91 Å | C/F=25-33 |
| 9JSW | EM | 1.94 Å | A/B/C/D/E/F/G/H=148-182 |
| 5EU3 | X-ray | 1.97 Å | C=280-288 |
| 5EU6 | X-ray | 2.02 Å | C=280-287 |
| 5EU4 | X-ray | 2.12 Å | C/F=280-288 |
| 6VM7 | X-ray | 2.41 Å | C=209-217 |
| 6VM8 | X-ray | 2.41 Å | C=209-217 |
| 4IS6 | X-ray | 2.5 Å | C=44-59 |
| 6VMA | X-ray | 2.75 Å | C=209-217 |
| 6VMC | X-ray | 2.85 Å | C=209-217 |
| 6VM9 | X-ray | 2.9 Å | C=209-217 |
| 7PHR | EM | 3.08 Å | P=280-288 |
| 9LIP | EM | 3.48 Å | A/E/I/M/Q/U/Y/c/g/k/o/s=66-89, B/F/J/N/R/V/Z/d/h/l/p/t=148-222, C/G/K/O/S/W/a/e/i/m/q/u=231-298, D/H/L/P/T/X/b/f/j/n/r/v=475-491 |
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