Tyrosine-protein kinase BTK (BTK) is a 659-residue protein from Homo sapiens. This is its AlphaFold structure prediction, created 1 Aug 2025. UniProt accession: Q06187.
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The mean pLDDT of this model is 84.4 (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 | 51% |
| 70 to 90 | Confident: backbone generally right | 35% |
| 50 to 70 | Low: treat with caution | 6% |
| Below 50 | Very low: often disordered regions | 7% |
What pLDDT means and how to read it
Non-receptor tyrosine kinase indispensable for B lymphocyte development, differentiation and signaling (PubMed:19290921). Binding of antigen to the B-cell antigen receptor (BCR) triggers signaling that ultimately leads to B-cell activation (PubMed:19290921). After BCR engagement and activation at the plasma membrane, phosphorylates PLCG2 at several sites, igniting the downstream signaling pathway through calcium mobilization, followed by activation of the protein kinase C (PKC) family members (PubMed:11606584). PLCG2 phosphorylation is performed in close cooperation with the adapter protein B-cell linker protein BLNK (PubMed:11606584). BTK acts as a platform to bring together a diverse…
Part of a complex composed of EEIG1, TNFRSF11A/RANK, PLCG2, GAB2, TEC and BTK; complex formation increases in the presence of TNFSF11/RANKL (By similarity). Binds GTF2I through the PH domain. Interacts with SH3BP5 via the SH3 domain. Interacts with IBTK via its PH domain. Interacts with ARID3A, CAV1, FASLG, PIN1, TLR8 and TLR9. Interacts with MPL/TPOR (PubMed:24607955). Interacts with STAC2;…
Cytoplasm, Cell membrane, Nucleus, Membrane raft
Compare the prediction with experimentally determined structures of the same protein:
| PDB ID | Method | Resolution | Chains and residues |
|---|---|---|---|
| 5P9J | X-ray | 1.08 Å | A=382-659 |
| 6DI1 | X-ray | 1.1 Å | A=389-659 |
| 5P9I | X-ray | 1.11 Å | A=382-659 |
| 6HRP | X-ray | 1.12 Å | A=378-659 |
| 6E4F | X-ray | 1.15 Å | A=387-659 |
| 4RFZ | X-ray | 1.17 Å | A=378-659 |
| 7L5O | X-ray | 1.21 Å | A=389-659 |
| 5P9L | X-ray | 1.25 Å | A=382-659 |
| 6DI9 | X-ray | 1.25 Å | A=389-659 |
| 6J6M | X-ray | 1.25 Å | A=393-659 |
| 7N5O | X-ray | 1.25 Å | A=382-659 |
| 5P9K | X-ray | 1.28 Å | A=382-659 |
| 6BLN | X-ray | 1.3 Å | A=393-657 |
| 6DI0 | X-ray | 1.3 Å | A=389-659 |
| 8FLV | X-ray | 1.3 Å | A=382-659 |
| 5U9D | X-ray | 1.33 Å | A=389-659 |
| 7KXM | X-ray | 1.33 Å | A=389-659 |
| 8FLN | X-ray | 1.33 Å | A=389-659 |
| 6X3P | X-ray | 1.34 Å | A=389-659 |
| 7KXN | X-ray | 1.34 Å | A=393-659 |
Showing 20 of 133 experimental structures (best resolution first).
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