Protein-tyrosine kinase 2-beta (PTK2B) is a 1009-residue protein from Homo sapiens. This is its AlphaFold structure prediction, created 1 Aug 2025. UniProt accession: Q14289.
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The mean pLDDT of this model is 76.2 (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 | 42% |
| 70 to 90 | Confident: backbone generally right | 29% |
| 50 to 70 | Low: treat with caution | 7% |
| Below 50 | Very low: often disordered regions | 21% |
What pLDDT means and how to read it
Non-receptor protein-tyrosine kinase that regulates reorganization of the actin cytoskeleton, cell polarization, cell migration, adhesion, spreading and bone remodeling. Plays a role in the regulation of the humoral immune response, and is required for normal levels of marginal B-cells in the spleen and normal migration of splenic B-cells. Required for normal macrophage polarization and migration towards sites of inflammation. Regulates cytoskeleton rearrangement and cell spreading in T-cells, and contributes to the regulation of T-cell responses. Promotes osteoclastic bone resorption; this requires both PTK2B/PYK2 and SRC. May inhibit differentiation and activity of osteoprogenitor cells.…
Homodimer, or homooligomer. Interacts with SIRPA and SH2D3C. Interacts with ARHGAP10. Interacts with DLG4 (By similarity). Interacts with KCNA2 (By similarity). Interacts with NPHP1, ASAP1, ASAP2, ARHGAP26, SKAP2 and TGFB1I1. The Tyr-402 phosphorylated form interacts with SRC (via SH2 domain) and SRC family members. Forms a signaling complex with EPHA1, LCK and phosphatidylinositol 3-kinase;…
Cytoplasm, Cytoplasm, perinuclear region, Cell membrane, Cell junction, focal adhesion, Cell projection, lamellipodium, Cytoplasm, cell cortex, Nucleus
Compare the prediction with experimentally determined structures of the same protein:
| PDB ID | Method | Resolution | Chains and residues |
|---|---|---|---|
| 3CC6 | X-ray | 1.6 Å | A=414-692 |
| 3FZS | X-ray | 1.75 Å | A=416-692 |
| 4XEK | X-ray | 1.79 Å | A=871-1005 |
| 8XOX | X-ray | 1.9 Å | A=416-692 |
| 3FZT | X-ray | 1.95 Å | A=416-692 |
| 5TO8 | X-ray | 1.98 Å | A=414-692 |
| 4H1M | X-ray | 1.99 Å | A=416-692 |
| 3H3C | X-ray | 2.0 Å | A=416-692 |
| 4H1J | X-ray | 2.0 Å | A=416-692 |
| 8YGX | X-ray | 2.0 Å | A=416-692 |
| 4XEV | X-ray | 2.01 Å | A/D=871-1005 |
| 3FZP | X-ray | 2.1 Å | A=416-692 |
| 5TOB | X-ray | 2.12 Å | A=414-692 |
| 3FZO | X-ray | 2.2 Å | A=416-692 |
| 4XEF | X-ray | 2.5 Å | A/D=871-1005 |
| 3GM3 | X-ray | 2.6 Å | A=861-1009 |
| 3ET7 | X-ray | 2.7 Å | A=416-692 |
| 3FZR | X-ray | 2.7 Å | A=416-692 |
| 3GM2 | X-ray | 2.71 Å | A=861-1009 |
| 3GM1 | X-ray | 2.95 Å | A/B=861-1009 |
Showing 20 of 26 experimental structures (best resolution first).
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