RAC-beta serine/threonine-protein kinase (AKT2) is a 481-residue protein from Homo sapiens. This is its AlphaFold structure prediction, created 1 Aug 2025. UniProt accession: P31751.
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The mean pLDDT of this model is 82.3 (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 | 50% |
| 70 to 90 | Confident: backbone generally right | 32% |
| 50 to 70 | Low: treat with caution | 8% |
| Below 50 | Very low: often disordered regions | 10% |
What pLDDT means and how to read it
Serine/threonine kinase closely related to AKT1 and AKT3. All 3 enzymes, AKT1, AKT2 and AKT3, are collectively known as AKT kinase. AKT regulates many processes including metabolism, proliferation, cell survival, growth and angiogenesis, through the phosphorylation of a range of downstream substrates. Over 100 substrates have been reported so far, although for most of them, the precise AKT kinase catalyzing the reaction was not specified. AKT regulates glucose uptake by mediating insulin-induced translocation of the SLC2A4/GLUT4 glucose transporter to the cell surface. Phosphorylation of PTPN1 at 'Ser-50' negatively modulates its phosphatase activity preventing dephosphorylation of the…
Interacts with BTBD10 (By similarity). Interacts with KCTD20 (By similarity). Interacts (via PH domain) with MTCP1, TCL1A and TCL1B; this interaction may facilitate AKT2 oligomerization and phosphorylation, hence increasing kinase activity (PubMed:10983986). Interacts with PHB2; this interaction may be important for myogenic differentiation (By similarity). Interacts (when phosphorylated) with…
Cytoplasm, Nucleus, Cell membrane, Early endosome
Compare the prediction with experimentally determined structures of the same protein:
| PDB ID | Method | Resolution | Chains and residues |
|---|---|---|---|
| 1O6L | X-ray | 1.6 Å | A=146-477 |
| 1O6K | X-ray | 1.7 Å | A=146-481 |
| 2JDO | X-ray | 1.8 Å | A=146-477 |
| 2X39 | X-ray | 1.93 Å | A=146-477 |
| 3D0E | X-ray | 2.0 Å | A/B=146-480 |
| 9C1W | X-ray | 2.0 Å | A=2-447 |
| 2UW9 | X-ray | 2.1 Å | A=146-477 |
| 1GZK | X-ray | 2.3 Å | A=146-460 |
| 2JDR | X-ray | 2.3 Å | A=146-477 |
| 3E87 | X-ray | 2.3 Å | A/B=146-480 |
| 8Q61 | X-ray | 2.32 Å | A=1-481 |
| 1GZN | X-ray | 2.5 Å | A=146-480 |
| 3E88 | X-ray | 2.5 Å | A/B=146-480 |
| 3E8D | X-ray | 2.7 Å | A/B=146-480 |
| 2XH5 | X-ray | 2.72 Å | A=146-479 |
| 1GZO | X-ray | 2.75 Å | A=146-460 |
| 1MRV | X-ray | 2.8 Å | A=143-481 |
| 1MRY | X-ray | 2.8 Å | A=143-481 |
| 1P6S | NMR | A=1-111 |
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