Alpha-synuclein (SNCA) is a 140-residue protein from Homo sapiens. This is its AlphaFold structure prediction, created 1 Aug 2025. UniProt accession: P37840.
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The mean pLDDT of this model is 75.2 (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 | 29% |
| 70 to 90 | Confident: backbone generally right | 34% |
| 50 to 70 | Low: treat with caution | 24% |
| Below 50 | Very low: often disordered regions | 13% |
What pLDDT means and how to read it
Neuronal protein that plays several roles in synaptic activity such as regulation of synaptic vesicle trafficking and subsequent neurotransmitter release (PubMed:20798282, PubMed:26442590, PubMed:28288128, PubMed:30404828). Participates as a monomer in synaptic vesicle exocytosis by enhancing vesicle priming, fusion and dilation of exocytotic fusion pores (PubMed:28288128, PubMed:30404828). Mechanistically, acts by increasing local Ca(2+) release from microdomains which is essential for the enhancement of ATP-induced exocytosis (PubMed:30404828). Also acts as a molecular chaperone in its multimeric membrane-bound state, assisting in the folding of synaptic fusion components called SNAREs…
Soluble monomer. Homotetramer (PubMed:21841800). A dynamic intracellular population of tetramers and monomers coexists normally and the tetramer plays an essential role in maintaining homeostasis (PubMed:21841800). Interacts with UCHL1 (By similarity). Interacts with phospholipase D and histones. Interacts (via N-terminus) with synphilin-1/SNCAIP; this interaction promotes formation of SNCA…
Cytoplasm, Membrane, Nucleus, Synapse, Secreted, Cell projection, axon
Compare the prediction with experimentally determined structures of the same protein:
| PDB ID | Method | Resolution | Chains and residues |
|---|---|---|---|
| 8JJV | X-ray | 1.23 Å | B=43-56 |
| 8JLY | X-ray | 1.29 Å | B=43-56 |
| 3Q27 | X-ray | 1.3 Å | A=32-57 |
| 4R0U | X-ray | 1.38 Å | A=72-78 |
| 6I42 | X-ray | 1.38 Å | B=48-60 |
| 4ZNN | EM | 1.41 Å | A=47-56 |
| 4RIL | EM | 1.43 Å | A=68-78 |
| 4R0W | X-ray | 1.5 Å | A=70-76 |
| 3Q26 | X-ray | 1.54 Å | A=10-42 |
| 3Q28 | X-ray | 1.6 Å | A=58-79 |
| 5CRW | X-ray | 1.6 Å | B=31-41 |
| 2X6M | X-ray | 1.62 Å | B=132-140 |
| 8OG0 | X-ray | 1.71 Å | P=136-140 |
| 8ZVY | X-ray | 1.72 Å | C/D=121-140 |
| 4RIK | X-ray | 1.85 Å | A=69-77 |
| 3Q25 | X-ray | 1.9 Å | A=1-19 |
| 6CT7 | X-ray | 1.9 Å | S/T=1-10 |
| 9EUU | EM | 1.93 Å | A/B/C/D/E/F/G/H/I/J/K/L/M/N/O/P/Q/R=1-140 |
| 8BQV | EM | 2.0 Å | A=1-140 |
| 9CK3 | EM | 2.04 Å | A/B/C/D/E/F/G/H/I/J/K/L=1-140 |
Showing 20 of 227 experimental structures (best resolution first).
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