Serine/threonine-protein kinase 24 (STK24) is a 443-residue protein from Homo sapiens. This is its AlphaFold structure prediction, created 1 Aug 2025. UniProt accession: Q9Y6E0.
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The mean pLDDT of this model is 77.6 (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 | 49% |
| 70 to 90 | Confident: backbone generally right | 24% |
| 50 to 70 | Low: treat with caution | 6% |
| Below 50 | Very low: often disordered regions | 22% |
What pLDDT means and how to read it
Serine/threonine-protein kinase that acts on both serine and threonine residues and promotes apoptosis in response to stress stimuli and caspase activation. Mediates oxidative-stress-induced cell death by modulating phosphorylation of JNK1-JNK2 (MAPK8 and MAPK9), p38 (MAPK11, MAPK12, MAPK13 and MAPK14) during oxidative stress. Plays a role in a staurosporine-induced caspase-independent apoptotic pathway by regulating the nuclear translocation of AIFM1 and ENDOG and the DNase activity associated with ENDOG. Phosphorylates STK38L on 'Thr-442' and stimulates its kinase activity. In association with STK26 negatively regulates Golgi reorientation in polarized cell migration upon RHO activation…
Monomer (PubMed:20124694). Interacts with CTTNBP2NL (PubMed:18782753). Interacts with RIPOR1 (via C-terminus); this interaction occurs in a PDCD10-dependent and Rho-independent manner (PubMed:27807006). Interacts with PDCD10; this interaction is required for the association of STK24 with RIPOR1 (PubMed:27807006). Part of the core of STRIPAK complexes composed of PP2A catalytic and scaffolding…
Cytoplasm, Nucleus, Membrane
Compare the prediction with experimentally determined structures of the same protein:
| PDB ID | Method | Resolution | Chains and residues |
|---|---|---|---|
| 3A7I | X-ray | 1.45 Å | A=10-315 |
| 8QLT | X-ray | 1.47 Å | A=4-301 |
| 3A7J | X-ray | 1.5 Å | A=10-315 |
| 4QMT | X-ray | 1.5 Å | A=10-315 |
| 3A7F | X-ray | 1.55 Å | A=10-315 |
| 4QMU | X-ray | 1.55 Å | A=10-315 |
| 4QMW | X-ray | 1.6 Å | A=10-315 |
| 8QLS | X-ray | 1.61 Å | A=4-301 |
| 4U8Z | X-ray | 1.63 Å | A=24-310 |
| 8QLQ | X-ray | 1.64 Å | A=4-301 |
| 8BZI | X-ray | 1.72 Å | A=4-301 |
| 7B32 | X-ray | 1.75 Å | A=4-301 |
| 4QMQ | X-ray | 1.77 Å | A=10-315 |
| 4W8D | X-ray | 1.77 Å | A=24-310 |
| 4W8E | X-ray | 1.79 Å | A=24-311 |
| 7B31 | X-ray | 1.8 Å | A=4-301 |
| 4QMM | X-ray | 1.85 Å | A=10-315 |
| 4QNA | X-ray | 1.85 Å | A=10-315 |
| 8QLR | X-ray | 1.85 Å | A/B=4-301 |
| 4QML | X-ray | 1.88 Å | A=10-315 |
Showing 20 of 40 experimental structures (best resolution first).
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