Wilms tumor protein (WT1) is a 449-residue protein from Homo sapiens. This is its AlphaFold structure prediction, created 1 Aug 2025. UniProt accession: P19544.
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The mean pLDDT of this model is 50.8 (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 | 9% |
| 70 to 90 | Confident: backbone generally right | 19% |
| 50 to 70 | Low: treat with caution | 7% |
| Below 50 | Very low: often disordered regions | 65% |
What pLDDT means and how to read it
Transcription factor that plays an important role in cellular development and cell survival (PubMed:7862533). Recognizes and binds to the DNA sequence 5'-GCG(T/G)GGGCG-3' (PubMed:17716689, PubMed:25258363, PubMed:7862533). Regulates the expression of numerous target genes, including EPO. Plays an essential role for development of the urogenital system. It has a tumor suppressor as well as an oncogenic role in tumor formation. Function may be isoform-specific: isoforms lacking the KTS motif may act as transcription factors (PubMed:15520190). Isoforms containing the KTS motif may bind mRNA and play a role in mRNA metabolism or splicing (PubMed:16934801). Isoform 1 has lower affinity for DNA,…
Homodimer. Interacts with WTIP. Interacts with actively translating polysomes. Detected in nuclear ribonucleoprotein (mRNP) particles. Interacts with HNRNPU via the zinc-finger region. Interacts with U2AF2. Interacts with CITED2 (By similarity). Interacts with ZNF224 via the zinc-finger region. Interacts with WTAP and SRY. Interacts with AMER1. Interacts with RBM4
Nucleus, Nucleus, nucleolus, Cytoplasm, Nucleus speckle, Nucleus, nucleoplasm
Compare the prediction with experimentally determined structures of the same protein:
| PDB ID | Method | Resolution | Chains and residues |
|---|---|---|---|
| 5KL3 | X-ray | 1.45 Å | A=350-440 |
| 4R2Q | X-ray | 1.54 Å | A=350-440 |
| 6B0O | X-ray | 1.55 Å | A/D=321-440 |
| 5KL7 | X-ray | 1.58 Å | A=350-440 |
| 5KL6 | X-ray | 1.64 Å | A=350-440 |
| 5KL2 | X-ray | 1.69 Å | A=350-440 |
| 5KL4 | X-ray | 1.78 Å | A/D=350-440 |
| 4R2P | X-ray | 1.79 Å | A=350-440 |
| 6B0R | X-ray | 1.82 Å | A/D=321-440 |
| 6BLW | X-ray | 1.83 Å | A=319-440 |
| 4R2E | X-ray | 1.84 Å | A=350-440 |
| 3MYJ | X-ray | 1.89 Å | C/F=126-134 |
| 3HPJ | X-ray | 2.0 Å | C/F=126-134 |
| 6B0P | X-ray | 2.08 Å | A/D=321-440 |
| 4R2R | X-ray | 2.09 Å | A=350-440 |
| 5KL5 | X-ray | 2.29 Å | A=350-440 |
| 8ISN | X-ray | 2.48 Å | C/F=235-243 |
| 4R2S | X-ray | 2.49 Å | A=350-440 |
| 7BBG | X-ray | 2.64 Å | C=126-134 |
| 6B0Q | X-ray | 2.79 Å | A/D=321-440 |
Showing 20 of 27 experimental structures (best resolution first).
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