P40344: Autophagy-related protein 3 (ATG3)

Autophagy-related protein 3 (ATG3) is a 310-residue protein from Saccharomyces cerevisiae (strain ATCC 204508 / S288c). This is its AlphaFold structure prediction, created 1 Aug 2025. UniProt accession: P40344.

Gene
ATG3
Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Length
310 residues
Mean pLDDT
73.4
Model
AF-P40344-F1 v6
Model created
1 Aug 2025
PDB structures
4

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Model confidence (pLDDT)

The mean pLDDT of this model is 73.4 (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 accurate47%
70 to 90Confident: backbone generally right17%
50 to 70Low: treat with caution8%
Below 50Very low: often disordered regions29%

What pLDDT means and how to read it

Function

E2 conjugating enzyme required for the cytoplasm to vacuole transport (Cvt) and autophagy. Required for selective autophagic degradation of the nucleus (nucleophagy) as well as for mitophagy which contributes to regulate mitochondrial quantity and quality by eliminating the mitochondria to a basal level to fulfill cellular energy requirements and preventing excess ROS production. Responsible for the E2-like covalent binding of phosphatidylethanolamine to the C-terminal Gly of ATG8. The ATG12-ATG5 conjugate plays a role of an E3 and promotes the transfer of ATG8 from ATG3 to phosphatidylethanolamine (PE). This step is required for the membrane association of ATG8. The formation of the…

Subunit structure

Monomer. Interacts with ATG8 through an intermediate thioester bond between Cys-234 and the C-terminal Gly of ATG8. Also interacts with the 40 amino acid C-terminal region of the E1-like ATG7 enzyme. Also interacts with the ATG12-ATG5 conjugate

Subcellular location

Cytoplasm, Mitochondrion

Experimental structures in the PDB

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

PDB IDMethodResolutionChains and residues
3T7GX-ray2.08 ÅC/D=128-144
6OJJX-ray2.41 ÅA=19-310
2DYTX-ray2.5 ÅA=1-310
4GSLX-ray2.7 ÅC/D=1-310

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