P46976: Glycogenin-1 (GYG1)

Glycogenin-1 (GYG1) is a 350-residue protein from Homo sapiens. This is its AlphaFold structure prediction, created 1 Aug 2025. UniProt accession: P46976.

Gene
GYG1
Organism
Homo sapiens
Length
350 residues
Mean pLDDT
84.3
Model
AF-P46976-F1 v6
Model created
1 Aug 2025
PDB structures
23

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Model confidence (pLDDT)

The mean pLDDT of this model is 84.3 (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 bandMeaningShare of residues
Above 90Very high: backbone and side chains are usually accurate57%
70 to 90Confident: backbone generally right24%
50 to 70Low: treat with caution10%
Below 50Very low: often disordered regions8%

What pLDDT means and how to read it

Function

Glycogenin participates in the glycogen biosynthetic process along with glycogen synthase and glycogen branching enzyme. It catalyzes the formation of a short alpha (1,4)-glucosyl chain covalently attached via a glucose 1-O-tyrosyl linkage to internal tyrosine residues and these chains act as primers for the elongation reaction catalyzed by glycogen synthase

Subunit structure

Part of the GYS1-GYG1 complex, a heterooctamer composed of a tetramer of GYS1 and 2 dimers of GYG1, where each GYS1 protomer binds to one GYG1 subunit (via GYG1 C-terminus); the GYS1 tetramer may dissociate from GYG1 dimers to continue glycogen polymerization on its own (PubMed:17055998, PubMed:22160680, PubMed:35690592, PubMed:35835870). May also form a heterooctamer complex with GYS2 (via GYG1…

Subcellular location

Cytoplasm, Nucleus

Disease associations

Experimental structures in the PDB

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

PDB IDMethodResolutionChains and residues
3U2UX-ray1.45 ÅA/B=1-262
3U2VX-ray1.5 ÅA/B=1-262
3U2WX-ray1.68 ÅA/B=1-262
7OVXX-ray1.7 ÅQ=339-350
3U2XX-ray1.77 ÅA/B=1-262
3T7MX-ray1.8 ÅA/B=1-262
3RMVX-ray1.82 ÅA=1-262
3T7OX-ray1.85 ÅA/B=1-262
3RMWX-ray1.93 ÅA=1-262
3Q4SX-ray1.98 ÅA=1-262
3T7NX-ray1.98 ÅA/B=1-262
3U2TX-ray2.05 ÅA=1-262
6EQJX-ray2.18 ÅA=1-262
3QVBX-ray2.26 ÅA=1-262
6EQLX-ray2.38 ÅA/B=1-262
7ZBNEM2.62 ÅE/F/G/H=1-350
7Q0BEM3.0 ÅE/F/G/H=1-350
7Q13EM3.0 ÅE/F/G/H=1-350
8CVXEM3.5 ÅE/F/G/H=1-350
8CVZEM3.52 ÅE/F/G/H/I/J=1-350

Showing 20 of 23 experimental structures (best resolution first).

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