Tyrosine-protein phosphatase non-receptor type 11 (PTPN11) is a 593-residue protein from Homo sapiens. This is its AlphaFold structure prediction, created 1 Aug 2025. UniProt accession: Q06124.
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The mean pLDDT of this model is 85.9 (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 | 63% |
| 70 to 90 | Confident: backbone generally right | 22% |
| 50 to 70 | Low: treat with caution | 4% |
| Below 50 | Very low: often disordered regions | 11% |
What pLDDT means and how to read it
Acts downstream of various receptor and cytoplasmic protein tyrosine kinases to participate in the signal transduction from the cell surface to the nucleus (PubMed:10655584, PubMed:14739280, PubMed:18559669, PubMed:18829466, PubMed:26742426, PubMed:28074573, PubMed:32184441). Positively regulates MAPK signal transduction pathway (PubMed:28074573). Dephosphorylates GAB1, ARHGAP35 and EGFR (PubMed:28074573). Dephosphorylates ROCK2 at 'Tyr-722' resulting in stimulation of its RhoA binding activity (PubMed:18559669). Dephosphorylates CDC73 (PubMed:26742426). Dephosphorylates SOX9 on tyrosine residues, leading to inactivate SOX9 and promote ossification (By similarity). Dephosphorylates…
Interacts with phosphorylated LIME1 and BCAR3. Interacts with SHB and INPP5D/SHIP1 (By similarity). Interacts with MILR1 (tyrosine-phosphorylated). Interacts with FLT1 (tyrosine-phosphorylated), FLT3 (tyrosine-phosphorylated), FLT4 (tyrosine-phosphorylated), KIT and GRB2. Interacts with PDGFRA (tyrosine phosphorylated). Interacts (via SH2 domain) with TEK/TIE2 (tyrosine phosphorylated) (By…
Cytoplasm, Nucleus
Compare the prediction with experimentally determined structures of the same protein:
| PDB ID | Method | Resolution | Chains and residues |
|---|---|---|---|
| 9EIK | X-ray | 1.25 Å | A=1-106 |
| 3ZM1 | X-ray | 1.4 Å | A=248-527 |
| 4JMG | X-ray | 1.4 Å | B=575-587 |
| 7PPM | X-ray | 1.48 Å | A=246-314, A=324-528 |
| 3ZM0 | X-ray | 1.5 Å | A=248-527 |
| 3ZM2 | X-ray | 1.5 Å | A=248-527 |
| 3ZM3 | X-ray | 1.5 Å | A=248-527 |
| 7PPL | X-ray | 1.53 Å | A=246-314, A=324-528 |
| 9EIC | X-ray | 1.58 Å | A=1-106 |
| 9EHD | X-ray | 1.59 Å | A=1-106 |
| 3B7O | X-ray | 1.6 Å | A=237-529 |
| 4RDD | X-ray | 1.6 Å | A=262-528 |
| 5EHR | X-ray | 1.7 Å | A/B=1-525 |
| 9MQ5 | X-ray | 1.7 Å | A=1-220 |
| 9EHA | X-ray | 1.71 Å | A=1-106 |
| 9Z70 | X-ray | 1.73 Å | A=4-103 |
| 5DF6 | X-ray | 1.78 Å | A=1-222 |
| 3TKZ | X-ray | 1.8 Å | A=1-106 |
| 6CMP | X-ray | 1.8 Å | A/B=1-529 |
| 7RCT | X-ray | 1.8 Å | A/B=1-525 |
Showing 20 of 115 experimental structures (best resolution first).
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