Synaptosomal-associated protein 25 (Snap25) is a 206-residue protein from Rattus norvegicus. This is its AlphaFold structure prediction, created 1 Aug 2025. UniProt accession: P60881.
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The mean pLDDT of this model is 83.7 (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 | 58% |
| 70 to 90 | Confident: backbone generally right | 22% |
| 50 to 70 | Low: treat with caution | 10% |
| Below 50 | Very low: often disordered regions | 11% |
What pLDDT means and how to read it
t-SNARE involved in the molecular regulation of neurotransmitter release (PubMed:8103915, PubMed:8243676). May play an important role in the synaptic function of specific neuronal systems. Associates with proteins involved in vesicle docking and membrane fusion. Regulates plasma membrane recycling through its interaction with CENPF. Modulates the gating characteristics of the delayed rectifier voltage-dependent potassium channel KCNB1 in pancreatic beta cells (PubMed:12403834)
Part of the SNARE core complex containing SNAP25, VAMP2 and STX1A;this complex constitutes the basic catalytic machinery of the complex neurotransmitter release apparatus (PubMed:12496247, PubMed:19196426, PubMed:9759724). Recruited to the SNARE complex following binding of the SNARE complex component STX1A to STXBP1 (By similarity). This complex binds CPLX1 (PubMed:12496247, PubMed:19196426,…
Cytoplasm, perinuclear region, Cell membrane, Synapse, synaptosome, Photoreceptor inner segment
Compare the prediction with experimentally determined structures of the same protein:
| PDB ID | Method | Resolution | Chains and residues |
|---|---|---|---|
| 1N7S | X-ray | 1.45 Å | C=7-83, D=141-204 |
| 5W5C | X-ray | 1.85 Å | C=7-83, D=141-204 |
| 1JTH | X-ray | 2.0 Å | A/C=1-82 |
| 1URQ | X-ray | 2.0 Å | C=5-83, D=141-204 |
| 6WVW | X-ray | 2.11 Å | C/G=10-83, D/H=141-204 |
| 1SFC | X-ray | 2.4 Å | C/G/K=1-83, D/H/L=120-206 |
| 5W5D | X-ray | 2.5 Å | C=7-83, D=141-204 |
| 5LOW | X-ray | 2.8 Å | D/F/K/M=7-82, E/G/L/N=141-203 |
| 9OJR | EM | 2.95 Å | H=1-83 |
| 9OJU | EM | 2.97 Å | H=1-83 |
| 9PFF | EM | 3.09 Å | G/I=1-83 |
| 5LOB | X-ray | 3.3 Å | D/F=7-82, E/G=141-203 |
| 9OJZ | EM | 3.39 Å | I=1-206 |
| 3HD7 | X-ray | 3.4 Å | C/G=7-83, D/H=141-204 |
| 9PB9 | EM | 3.45 Å | I=1-206 |
| 9PBA | EM | 3.47 Å | I=1-206 |
| 5CCG | X-ray | 3.5 Å | C/I=7-83, D/J=141-204 |
| 5KJ7 | X-ray | 3.5 Å | C/I=9-83, D/J=141-204 |
| 9OLO | EM | 3.56 Å | I/J=1-206 |
| 9PFG | EM | 3.58 Å | A/C=1-83 |
Showing 20 of 45 experimental structures (best resolution first).
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