Tenascin (TNC) is a 2201-residue protein from Homo sapiens. This is its AlphaFold structure prediction, created 1 Aug 2025. UniProt accession: P24821.
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The mean pLDDT of this model is 74.9 (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 | 9% |
| 70 to 90 | Confident: backbone generally right | 64% |
| 50 to 70 | Low: treat with caution | 21% |
| Below 50 | Very low: often disordered regions | 7% |
What pLDDT means and how to read it
Extracellular matrix protein implicated in guidance of migrating neurons as well as axons during development, synaptic plasticity as well as neuronal regeneration. Promotes neurite outgrowth from cortical neurons grown on a monolayer of astrocytes. Ligand for integrins alpha-8/beta-1, alpha-9/beta-1, alpha-V/beta-3 and alpha-V/beta-6. In tumors, stimulates angiogenesis by elongation, migration and sprouting of endothelial cells (PubMed:19884327)
Homohexamer; disulfide-linked. A homotrimer may be formed in the triple coiled-coil region and may be stabilized by disulfide rings at both ends. Two of such half-hexabrachions may be disulfide linked within the central globule. Interacts with CSPG4 (PubMed:8824254). Interacts (via the 3rd fibronectin type-III domain) with integrin ITGA9:ITGB1 (PubMed:22654117)
Secreted, extracellular space, extracellular matrix
Compare the prediction with experimentally determined structures of the same protein:
| PDB ID | Method | Resolution | Chains and residues |
|---|---|---|---|
| 5R61 | X-ray | 1.38 Å | A=1979-2196 |
| 5R62 | X-ray | 1.4 Å | A=1979-2196 |
| 6QNV | X-ray | 1.4 Å | A=1979-2196 |
| 9R5Y | X-ray | 1.4 Å | A/D=1976-2193 |
| 2RB8 | X-ray | 1.45 Å | A=802-893 |
| 5R5U | X-ray | 1.52 Å | A=1979-2196 |
| 5R5T | X-ray | 1.55 Å | A=1979-2196 |
| 5R5X | X-ray | 1.56 Å | A=1979-2196 |
| 5R5Y | X-ray | 1.57 Å | A=1979-2196 |
| 5R63 | X-ray | 1.59 Å | A=1979-2196 |
| 5R5W | X-ray | 1.6 Å | A=1979-2196 |
| 5R5Z | X-ray | 1.67 Å | A=1979-2196 |
| 5R5V | X-ray | 1.7 Å | A=1979-2196 |
| 5R60 | X-ray | 1.79 Å | A=1979-2196 |
| 1TEN | X-ray | 1.8 Å | A=802-891 |
| 8FNB | X-ray | 1.8 Å | A/B=1975-2201 |
| 8FN8 | X-ray | 1.89 Å | A=1975-2201 |
| 2RBL | X-ray | 2.1 Å | A/B/M=802-893 |
| 9NIH | X-ray | 2.4 Å | C=1013-1024 |
| 6BRB | X-ray | 2.82 Å | D=809-893 |
Showing 20 of 21 experimental structures (best resolution first).
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