Q9WV60: Glycogen synthase kinase-3 beta (Gsk3b)

Glycogen synthase kinase-3 beta (Gsk3b) is a 420-residue protein from Mus musculus. This is its AlphaFold structure prediction, created 1 Aug 2025. UniProt accession: Q9WV60.

Gene
Gsk3b
Organism
Mus musculus
Length
420 residues
Mean pLDDT
88.1
Model
AF-Q9WV60-F1 v6
Model created
1 Aug 2025
PDB structures
6

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Model confidence (pLDDT)

The mean pLDDT of this model is 88.1 (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 accurate78%
70 to 90Confident: backbone generally right8%
50 to 70Low: treat with caution2%
Below 50Very low: often disordered regions12%

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), EIF2B, CTNNB1/beta-catenin, APC, AXIN1, DPYSL2/CRMP2, JUN, NFATC1/NFATC, MAPT/TAU and MACF1 (PubMed:15791206, PubMed:22057101, PubMed:23395175). Requires primed phosphorylation of the majority of its substrates (PubMed:15791206, PubMed:22057101, PubMed:23395175). In skeletal muscle, contributes to insulin regulation of glycogen synthesis by phosphorylating and inhibiting GYS1 activity and hence glycogen synthesis (By similarity). May…

Subunit structure

Monomer (By similarity). Interacts with DAB2IP (via C2 domain); the interaction stimulates GSK3B kinase activation (By similarity). Interacts (via C2 domain) with PPP2CA (By similarity). Interacts with CABYR, MMP2, MUC1, NIN and PRUNE1 (By similarity). Interacts with AXIN1; the interaction mediates hyperphosphorylation of CTNNB1 leading to its ubiquitination and destruction (PubMed:19141611).…

Subcellular location

Cytoplasm, Nucleus, Cell membrane

Experimental structures in the PDB

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

PDB IDMethodResolutionChains and residues
6AE3X-ray2.14 ÅA/B/C/D=1-420
8VMEX-ray2.3 ÅA=26-383
8VMGX-ray2.45 ÅA/B=26-383
4NU1X-ray2.5 ÅA=1-383
8VMFX-ray2.5 ÅA=26-383
5AIRX-ray2.53 ÅA/B=4-420

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