Activated CDC42 kinase 1 (TNK2) is a 1038-residue protein from Homo sapiens. This is its AlphaFold structure prediction, created 1 Aug 2025. UniProt accession: Q07912.
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The mean pLDDT of this model is 61.3 (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 | 30% |
| 70 to 90 | Confident: backbone generally right | 11% |
| 50 to 70 | Low: treat with caution | 10% |
| Below 50 | Very low: often disordered regions | 49% |
What pLDDT means and how to read it
Non-receptor tyrosine-protein and serine/threonine-protein kinase that is implicated in cell spreading and migration, cell survival, cell growth and proliferation. Transduces extracellular signals to cytosolic and nuclear effectors. Phosphorylates AKT1, AR, MCF2, WASL and WWOX. Implicated in trafficking and clathrin-mediated endocytosis through binding to epidermal growth factor receptor (EGFR) and clathrin. Binds to both poly- and mono-ubiquitin and regulates ligand-induced degradation of EGFR, thereby contributing to the accumulation of EGFR at the limiting membrane of early endosomes. Downstream effector of CDC42 which mediates CDC42-dependent cell migration via phosphorylation of…
Interacts with NEDD4 (via WW3 domain). NEDD4L and EGF promote association with NEDD4 (By similarity). Homodimer. Interacts with AR, CDC42, WWASL and WWOX. Interacts with CSPG4 (activated). Interacts with MERTK (activated); stimulates autophosphorylation. May interact (phosphorylated) with HSP90AB1; maintains kinase activity. Interacts with NPHP1. Interacts with SNX9 (via SH3 domain). Interacts…
Cell membrane, Nucleus, Endosome, Cell junction, adherens junction, Cytoplasmic vesicle membrane, Cytoplasmic vesicle, clathrin-coated vesicle, Membrane, clathrin-coated pit, Cytoplasm, perinuclear region, Cytoplasm, cytosol
Compare the prediction with experimentally determined structures of the same protein:
| PDB ID | Method | Resolution | Chains and residues |
|---|---|---|---|
| 4HZR | X-ray | 1.31 Å | A/B=115-389 |
| 8THA | X-ray | 1.68 Å | A=954-1038 |
| 7KP6 | X-ray | 1.79 Å | A/B=110-391 |
| 8Q5P | X-ray | 1.81 Å | B=508-519 |
| 1U46 | X-ray | 2.0 Å | A/B=109-395 |
| 3EQR | X-ray | 2.0 Å | A/B=117-392 |
| 1U4D | X-ray | 2.1 Å | A/B=109-395 |
| 5ZXB | X-ray | 2.2 Å | A/B=117-391 |
| 3EQP | X-ray | 2.3 Å | A/B=117-392 |
| 4EWH | X-ray | 2.5 Å | A/B=117-391 |
| 8FZ3 | X-ray | 2.78 Å | A/B/C/D=958-1038 |
| 1U54 | X-ray | 2.8 Å | A/B=109-395 |
| 6VQM | X-ray | 2.87 Å | A/B=109-395 |
| 4ID7 | X-ray | 3.0 Å | A=117-389 |
| 8HMT | X-ray | 3.17 Å | A/B/C/D=117-389 |
| 8FE9 | X-ray | 3.2 Å | A=110-391 |
| 4HZS | X-ray | 3.23 Å | A/B/C/D=115-453 |
| 1CF4 | NMR | B=446-489 |
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