Serine/threonine-protein kinase TBK1 (TBK1) is a 729-residue protein from Homo sapiens. This is its AlphaFold structure prediction, created 1 Aug 2025. UniProt accession: Q9UHD2.
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The mean pLDDT of this model is 89.7 (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 | 72% |
| 70 to 90 | Confident: backbone generally right | 19% |
| 50 to 70 | Low: treat with caution | 6% |
| Below 50 | Very low: often disordered regions | 4% |
What pLDDT means and how to read it
Serine/threonine kinase that plays an essential role in regulating inflammatory responses to foreign agents (PubMed:10581243, PubMed:11839743, PubMed:12692549, PubMed:12702806, PubMed:14703513, PubMed:15367631, PubMed:15485837, PubMed:18583960, PubMed:21138416, PubMed:23453971, PubMed:23453972, PubMed:23746807, PubMed:25636800, PubMed:26611359, PubMed:32404352, PubMed:34363755, PubMed:32298923). Following activation of toll-like receptors by viral or bacterial components, associates with TRAF3 and TANK and phosphorylates interferon regulatory factors (IRFs) IRF3 and IRF7 as well as DDX3X (PubMed:12692549, PubMed:12702806, PubMed:14703513, PubMed:15367631, PubMed:18583960, PubMed:25636800).…
Homodimer (PubMed:21145761, PubMed:37926288). Interacts with DDX3X, TIRAP and TRAF2 (PubMed:10581243, PubMed:14530355). Part of a ternary complex consisting of TANK, TRAF2 and TBK1 (PubMed:10581243). Interacts with AZI2, TANK and TBKBP1; these interactions are mutually exclusive and mediate TBK1 activation (PubMed:10581243, PubMed:14560022, PubMed:21931631, PubMed:23453972, PubMed:29251827).…
Cytoplasm
Compare the prediction with experimentally determined structures of the same protein:
| PDB ID | Method | Resolution | Chains and residues |
|---|---|---|---|
| 5EP6 | X-ray | 1.45 Å | B/D=677-729 |
| 4EFO | X-ray | 1.77 Å | A/B=302-383 |
| 4EUU | X-ray | 1.8 Å | A/B=2-308 |
| 5EOF | X-ray | 2.05 Å | C/D=677-729 |
| 4IM0 | X-ray | 2.4 Å | A=1-657 |
| 4IM2 | X-ray | 2.5 Å | A=1-657 |
| 5EOA | X-ray | 2.5 Å | C/D=677-729 |
| 4EUT | X-ray | 2.6 Å | A/B=2-385 |
| 4IWO | X-ray | 2.61 Å | A=2-657 |
| 6RSU | X-ray | 2.75 Å | A=2-657 |
| 4IWQ | X-ray | 3.0 Å | A=2-657 |
| 4IWP | X-ray | 3.06 Å | A=2-657 |
| 6RSR | X-ray | 3.15 Å | A=2-657 |
| 6CQ0 | X-ray | 3.19 Å | A=1-657 |
| 6BOD | X-ray | 3.2 Å | A=1-657 |
| 6CQ4 | X-ray | 3.2 Å | A=1-657 |
| 6RST | X-ray | 3.29 Å | A=2-657 |
| 6NT9 | EM | 3.3 Å | A/B=1-729 |
| 4IM3 | X-ray | 3.34 Å | A=1-657 |
| 6BNY | X-ray | 3.34 Å | A=1-657 |
Showing 20 of 25 experimental structures (best resolution first).
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