P49840: Glycogen synthase kinase-3 alpha (GSK3A)

Glycogen synthase kinase-3 alpha (GSK3A) is a 483-residue protein from Homo sapiens. This is its AlphaFold structure prediction, created 1 Aug 2025. UniProt accession: P49840.

Gene
GSK3A
Organism
Homo sapiens
Length
483 residues
Mean pLDDT
78.9
Model
AF-P49840-F1 v6
Model created
1 Aug 2025
PDB structures
2

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Model confidence (pLDDT)

The mean pLDDT of this model is 78.9 (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 bandMeaningShare of residues
Above 90Very high: backbone and side chains are usually accurate66%
70 to 90Confident: backbone generally right6%
50 to 70Low: treat with caution1%
Below 50Very low: often disordered regions27%

What pLDDT means and how to read it

Function

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), CTNNB1/beta-catenin, APC and AXIN1 (PubMed:11749387, PubMed:17478001, PubMed:19366350). Requires primed phosphorylation of the majority of its substrates (PubMed:11749387, PubMed:17478001, PubMed:19366350). Contributes to insulin regulation of glycogen synthesis by phosphorylating and inhibiting GYS1 activity and hence glycogen synthesis (PubMed:11749387, PubMed:17478001, PubMed:19366350). Regulates glycogen metabolism in liver, but…

Subunit structure

Monomer. Interacts with ARRB2 (By similarity). Interacts with AXIN1 and CTNNB1/beta-catenin (PubMed:17229088). Interacts with CTNND2 (PubMed:19706605). Interacts with LMBR1L (PubMed:31073040). Interacts with DDX3X (PubMed:18846110). Interacts with TNFRSF10B (PubMed:18846110). Interacts with RICTOR; the interaction results in phosphorylation of RICTOR at 'Thr-1695' by GSK3A which facilitates…

Experimental structures in the PDB

Compare the prediction with experimentally determined structures of the same protein:

PDB IDMethodResolutionChains and residues
7SXFX-ray1.94 ÅA=101-444
7SXGX-ray2.4 ÅA=103-445

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