Glycogen synthase kinase-3 beta (GSK3B) is a 420-residue protein from Homo sapiens. This is its AlphaFold structure prediction, created 1 Aug 2025. UniProt accession: P49841.
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The mean pLDDT of this model is 88.3 (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 | 77% |
| 70 to 90 | Confident: backbone generally right | 9% |
| 50 to 70 | Low: treat with caution | 1% |
| Below 50 | Very low: often disordered regions | 12% |
What pLDDT means and how to read it
Constitutively active protein kinase that acts as a negative regulator in the hormonal control of glucose homeostasis, Wnt signaling and regulation of transcription factors and microtubules, by phosphorylating and inactivating glycogen synthase (GYS1 or GYS2), EIF2B, CTNNB1/beta-catenin, APC, AXIN1, DPYSL2/CRMP2, JUN, NFATC1/NFATC, MAPT/TAU and MACF1 (PubMed:11430833, PubMed:12554650, PubMed:14690523, PubMed:16484495, PubMed:1846781, PubMed:20937854, PubMed:9072970). Requires primed phosphorylation of the majority of its substrates (PubMed:11430833, PubMed:16484495). In skeletal muscle, contributes to insulin regulation of glycogen synthesis by phosphorylating and inhibiting GYS1 activity…
Monomer. Interacts with ARRB2, DISC1 and ZBED3 (By similarity). Interacts with CABYR, MMP2, MUC1, NIN and PRUNE1. Interacts with AXIN1; the interaction mediates hyperphosphorylation of CTNNB1 leading to its ubiquitination and destruction. Interacts with and phosphorylates SNAI1. Interacts with DNM1L (via a C-terminal domain). Found in a complex composed of MACF1, APC, AXIN1, CTNNB1 and GSK3B (By…
Cytoplasm, Nucleus, Cell membrane
Compare the prediction with experimentally determined structures of the same protein:
| PDB ID | Method | Resolution | Chains and residues |
|---|---|---|---|
| 9X2V | X-ray | 1.39 Å | A=27-383 |
| 1O6L | X-ray | 1.6 Å | C=3-12 |
| 9X2Q | X-ray | 1.68 Å | A/C=27-383 |
| 1O6K | X-ray | 1.7 Å | C=3-12 |
| 9X2X | X-ray | 1.79 Å | A/C=27-383 |
| 1J1B | X-ray | 1.8 Å | A/B=1-420 |
| 2JDO | X-ray | 1.8 Å | C=3-12 |
| 7SXJ | X-ray | 1.85 Å | A=34-383 |
| 3QKL | X-ray | 1.9 Å | C=3-12 |
| 9X2W | X-ray | 1.92 Å | A/C=27-383 |
| 2X39 | X-ray | 1.93 Å | C=3-12 |
| 1Q5K | X-ray | 1.94 Å | A/B=7-420 |
| 9X2Y | X-ray | 1.96 Å | A/B=27-383 |
| 4AFJ | X-ray | 1.98 Å | A/B=27-393 |
| 3CQW | X-ray | 2.0 Å | C=3-12 |
| 4PTE | X-ray | 2.03 Å | A/B=1-420 |
| 6Y9S | X-ray | 2.03 Å | A/B=35-384 |
| 7B6F | X-ray | 2.05 Å | A=26-383 |
| 9X2U | X-ray | 2.07 Å | A/B=27-383 |
| 6Y9R | X-ray | 2.08 Å | A=35-384 |
Showing 20 of 122 experimental structures (best resolution first).
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