Dystroglycan 1 (DAG1) is a 895-residue protein from Homo sapiens. This is its AlphaFold structure prediction, created 1 Aug 2025. UniProt accession: Q14118.
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The mean pLDDT of this model is 68.2 (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 | 32% |
| 70 to 90 | Confident: backbone generally right | 21% |
| 50 to 70 | Low: treat with caution | 10% |
| Below 50 | Very low: often disordered regions | 38% |
What pLDDT means and how to read it
The dystroglycan complex is involved in a number of signaling events and processes including laminin deposition and extracellular matrix assembly, acetylcholine receptor clustering, sarcolemmal stability, cell survival, peripheral nerve myelination, nodal structure, cell migration, epithelial polarization, and epithelium branching morphogenesis (By similarity). Required for the formation of photoreceptor ribbon synapses, and long-term maintenance of inhibitory synapses in cerebellar Purkinje cells (By similarity). Also involved in the positive regulation of cartilage formation through agrin (AGRN) binding and up-regulation of SOX9, a transcription factor that plays a key role in…
Monomer. Heterodimer of alpha- and beta-dystroglycan subunits which are the central components of the dystrophin-glycoprotein complex. This complex then can form a dystrophin-associated glycoprotein complex (DGC) which is composed of three subcomplexes: a cytoplasmic complex comprised of DMD (or UTRN), DTNA and a number of syntrophins, such as SNTB1, SNTB2, SNTG1 and SNTG2, the transmembrane…
Secreted, extracellular space, Secreted, extracellular space, extracellular matrix, basement membrane, Synapse, Cell membrane, Cytoplasm, cytoskeleton, Nucleus, nucleoplasm, Cell membrane, sarcolemma, Postsynaptic cell membrane
Compare the prediction with experimentally determined structures of the same protein:
| PDB ID | Method | Resolution | Chains and residues |
|---|---|---|---|
| 5GGP | X-ray | 1.6 Å | C/D=316-325 |
| 5LLK | X-ray | 1.8 Å | A=52-315 |
| 1EG4 | X-ray | 2.0 Å | P=881-895 |
| 7E9K | X-ray | 2.05 Å | C/F=369-389 |
| 7E9L | X-ray | 2.1 Å | C=378-389 |
| 6JJY | X-ray | 2.3 Å | U=877-895 |
| 8UF4 | X-ray | 2.43 Å | A/C=491-653, B/D=654-748 |
| 2MK7 | NMR | A=418-427 |
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