Q9NT62: Ubiquitin-like-conjugating enzyme ATG3 (ATG3)

Ubiquitin-like-conjugating enzyme ATG3 (ATG3) is a 314-residue protein from Homo sapiens. This is its AlphaFold structure prediction, created 1 Aug 2025. UniProt accession: Q9NT62.

Gene
ATG3
Organism
Homo sapiens
Length
314 residues
Mean pLDDT
73.4
Model
AF-Q9NT62-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 accurate30%
70 to 90Confident: backbone generally right30%
50 to 70Low: treat with caution22%
Below 50Very low: often disordered regions19%

What pLDDT means and how to read it

Function

E2 conjugating enzyme that catalyzes the covalent conjugation of the C-terminal Gly of ATG8-like proteins (GABARAP, GABARAPL1, GABARAPL2 or MAP1LC3A) to the amino group of phosphatidylethanolamine (PE)-containing lipids in the membrane resulting in membrane-bound ATG8-like proteins which is one of the key steps in the development of autophagic isolation membranes during autophagosome formation (PubMed:24191030, PubMed:33446636, PubMed:37252361). Cycles back and forth between binding to ATG7 for loading with the ATG8-like proteins and binding to E3 enzyme, composed of ATG12, ATG5 and ATG16L1 to promote ATG8-like proteins lipidation (PubMed:11825910, PubMed:12207896, PubMed:12890687,…

Subunit structure

Homodimer (PubMed:24191030). Interacts with ATG7; this interaction forms an E1-E2 complex that is essential for the transfer of GABARAP thioester from ATG7 to ATG3 and disrupts interaction with the E3 enzyme complex (PubMed:11825910, PubMed:22170151, PubMed:24186333, PubMed:26043688, PubMed:37252361). Interacts with ATG12; this interaction is ATG7-dependent, essential for…

Subcellular location

Cytoplasm

Experimental structures in the PDB

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

PDB IDMethodResolutionChains and residues
4NAWX-ray2.2 ÅD/H/L/P=140-170
8AFIX-ray2.66 ÅB/D/F/H/J/L/N/P=90-113
9E8PX-ray2.7 ÅA/B=26-314
8FKMNMRA=25-314

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