Q9H1Y0: Autophagy protein 5 (ATG5)

Autophagy protein 5 (ATG5) is a 275-residue protein from Homo sapiens. This is its AlphaFold structure prediction, created 1 Aug 2025. UniProt accession: Q9H1Y0.

Gene
ATG5
Organism
Homo sapiens
Length
275 residues
Mean pLDDT
93.3
Model
AF-Q9H1Y0-F1 v6
Model created
1 Aug 2025
PDB structures
9

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Model confidence (pLDDT)

The mean pLDDT of this model is 93.3 (very high 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 accurate81%
70 to 90Confident: backbone generally right15%
50 to 70Low: treat with caution3%
Below 50Very low: often disordered regions0%

What pLDDT means and how to read it

Function

Involved in autophagic vesicle formation. Conjugation with ATG12, through a ubiquitin-like conjugating system involving ATG7 as an E1-like activating enzyme and ATG10 as an E2-like conjugating enzyme, is essential for its function. The ATG12-ATG5 conjugate acts as an E3-like enzyme which is required for lipidation of ATG8 family proteins and their association to the vesicle membranes. Involved in mitochondrial quality control after oxidative damage, and in subsequent cellular longevity. Plays a critical role in multiple aspects of lymphocyte development and is essential for both B and T lymphocyte survival and proliferation. Required for optimal processing and presentation of antigens for…

Subunit structure

Forms a conjugate with ATG12 (PubMed:11825910, PubMed:12207896, PubMed:17709747, PubMed:26812546). Part of the minor complex composed of 4 sets of ATG12-ATG5 and ATG16L1 (400 kDa); this complex interacts with ATG3 leading to disruption of ATG7 interaction and promotion of ATG8-like proteins lipidation (PubMed:24191030). Forms an 800-kDa complex composed of ATG12-ATG5 and ATG16L2 (By similarity).…

Subcellular location

Cytoplasm, Preautophagosomal structure membrane

Disease associations

Experimental structures in the PDB

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

PDB IDMethodResolutionChains and residues
4TQ1X-ray1.8 ÅA=1-275
4NAWX-ray2.2 ÅB/F/J/N=1-275
4GDKX-ray2.7 ÅB/E=1-275
4TQ0X-ray2.7 ÅA/C/E=1-275
4GDLX-ray2.88 ÅB=1-275
5D7GX-ray3.0 ÅA/C/E/G=1-275
7W36X-ray3.0 ÅA=1-275
5NPVX-ray3.1 ÅA/C=1-275
5NPWX-ray3.1 ÅA/C/E/G=1-275

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