Syntaxin-1A (Stx1a) is a 288-residue protein from Rattus norvegicus. This is its AlphaFold structure prediction, created 1 Aug 2025. UniProt accession: P32851.
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The mean pLDDT of this model is 84.7 (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 | 52% |
| 70 to 90 | Confident: backbone generally right | 30% |
| 50 to 70 | Low: treat with caution | 15% |
| Below 50 | Very low: often disordered regions | 4% |
What pLDDT means and how to read it
Plays an essential role in hormone and neurotransmitter calcium-dependent exocytosis and endocytosis (PubMed:17301173, PubMed:18167541, PubMed:20484665, PubMed:22411134, PubMed:28813412, PubMed:7901002). Part of the SNARE (Soluble NSF Attachment Receptor) complex composed of SNAP25, STX1A and VAMP2 which mediates the fusion of synaptic vesicles with the presynaptic plasma membrane (PubMed:14665625, PubMed:16888141, PubMed:19571812). STX1A and SNAP25 are localized on the plasma membrane while VAMP2 resides in synaptic vesicles. The pairing of the three SNAREs from the N-terminal SNARE motifs to the C-terminal anchors leads to the formation of the SNARE complex, which brings membranes into…
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:11533035, PubMed:11832227, PubMed:12496247, PubMed:14665625, PubMed:16888141, PubMed:18337752, PubMed:19196426, PubMed:19571812, PubMed:21785414, PubMed:26280336, PubMed:28813412, PubMed:9759724). The SNARE complex…
Cytoplasmic vesicle, secretory vesicle, synaptic vesicle membrane, Cell membrane, Synapse, synaptosome
Compare the prediction with experimentally determined structures of the same protein:
| PDB ID | Method | Resolution | Chains and residues |
|---|---|---|---|
| 1N7S | X-ray | 1.45 Å | B=191-256 |
| 5W5C | X-ray | 1.85 Å | B=190-256 |
| 1EZ3 | X-ray | 1.9 Å | A/B/C=24-150 |
| 1JTH | X-ray | 2.0 Å | B/D=191-267 |
| 1URQ | X-ray | 2.0 Å | B=185-259 |
| 6WVW | X-ray | 2.11 Å | B/F=191-256 |
| 3RK2 | X-ray | 2.2 Å | B/F=191-253 |
| 1KIL | X-ray | 2.3 Å | B=190-250 |
| 1HVV | X-ray | 2.4 Å | A/B/C/D=190-264 |
| 1SFC | X-ray | 2.4 Å | B/F/J=180-262 |
| 4JEH | X-ray | 2.5 Å | B=24-266 |
| 5W5D | X-ray | 2.5 Å | B=190-256 |
| 3C98 | X-ray | 2.6 Å | B=1-267 |
| 9PFF | EM | 3.09 Å | H/J=190-267 |
| 4JEU | X-ray | 3.2 Å | B=2-243 |
| 7XSJ | X-ray | 3.2 Å | B=25-267 |
| 9OJZ | EM | 3.39 Å | G/H=1-267 |
| 3HD7 | X-ray | 3.4 Å | B/F=183-288 |
| 9PB9 | EM | 3.45 Å | G/H=1-267 |
| 9PBA | EM | 3.47 Å | G/H=1-267 |
Showing 20 of 54 experimental structures (best resolution first).
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