Tyrosine-protein kinase JAK2 (JAK2) is a 1132-residue protein from Homo sapiens. This is its AlphaFold structure prediction, created 1 Aug 2025. UniProt accession: O60674.
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The mean pLDDT of this model is 86.9 (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 | 67% |
| 70 to 90 | Confident: backbone generally right | 22% |
| 50 to 70 | Low: treat with caution | 4% |
| Below 50 | Very low: often disordered regions | 6% |
What pLDDT means and how to read it
Non-membrane spanning protein tyrosine kinase that phosphorylates type I receptors such as growth hormone (GHR), prolactin (PRLR), leptin (LEPR), erythropoietin (EPOR), thrombopoietin receptor (MPL/TPOR); or type II receptors including IFN-alpha, IFN-beta, IFN-gamma and multiple interleukins (PubMed:15690087, PubMed:15899890, PubMed:7615558, PubMed:9188471, PubMed:9657743). Functionally, plays a pivotal role in signal transduction and is involved in various processes such as cell growth, development, differentiation or histone modifications. Mediates essential signaling events in both innate and adaptive immunity. Mechanistically, following ligand-binding to cell surface receptors,…
Interacts with EPOR, LYN, SIRPA, SH2B1 and TEC (By similarity). Interacts with IL23R (PubMed:12023369). Interacts with SKB1 (PubMed:10531356). Interacts with STAM2 (PubMed:10899310). Interacts with IFNGR2 (via intracellular domain) (PubMed:7615558, PubMed:7673114). Interacts with LEPR (Isoform B) (By similarity). Interacts with HSP90AB1; promotes functional activation in a heat shock-dependent…
Endomembrane system, Cytoplasm, Nucleus
Compare the prediction with experimentally determined structures of the same protein:
| PDB ID | Method | Resolution | Chains and residues |
|---|---|---|---|
| 8BXH | X-ray | 1.3 Å | A=840-1132 |
| 7LL4 | X-ray | 1.31 Å | A=839-1132 |
| 3UGC | X-ray | 1.34 Å | A=840-1132 |
| 7REE | X-ray | 1.38 Å | A=839-1132 |
| 8BA3 | X-ray | 1.4 Å | A=536-812 |
| 8BX9 | X-ray | 1.4 Å | A/B=840-1132 |
| 7TEU | X-ray | 1.45 Å | A=837-1132 |
| 4IVA | X-ray | 1.5 Å | A=833-1132 |
| 5UT3 | X-ray | 1.5 Å | A=536-812 |
| 7LL5 | X-ray | 1.5 Å | A=840-1132 |
| 7RN6 | X-ray | 1.5 Å | A=839-1132 |
| 8B8U | X-ray | 1.5 Å | A/B=536-812 |
| 8B9E | X-ray | 1.5 Å | A=536-812 |
| 8B9H | X-ray | 1.5 Å | A=536-812 |
| 8BA2 | X-ray | 1.5 Å | A=536-812 |
| 8BM2 | X-ray | 1.5 Å | A/B=840-1132 |
| 8BX6 | X-ray | 1.5 Å | A=840-1132 |
| 8EX1 | X-ray | 1.5 Å | A=536-812 |
| 5I4N | X-ray | 1.54 Å | A=535-812 |
| 6BS0 | X-ray | 1.54 Å | A=536-812 |
Showing 20 of 164 experimental structures (best resolution first).
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