O94817: Ubiquitin-like protein ATG12 (ATG12)

Ubiquitin-like protein ATG12 (ATG12) is a 140-residue protein from Homo sapiens. This is its AlphaFold structure prediction, created 1 Aug 2025. UniProt accession: O94817.

Gene
ATG12
Organism
Homo sapiens
Length
140 residues
Mean pLDDT
78.9
Model
AF-O94817-F1 v6
Model created
1 Aug 2025
PDB structures
3

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Model confidence (pLDDT)

The mean pLDDT of this model is 78.9 (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 accurate55%
70 to 90Confident: backbone generally right9%
50 to 70Low: treat with caution26%
Below 50Very low: often disordered regions10%

What pLDDT means and how to read it

Function

Ubiquitin-like protein involved in autophagy vesicles formation. Conjugation with ATG5 through a ubiquitin-like conjugating system involving also 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. As part of the ATG8 conjugation system with ATG5 and ATG16L1, required for recruitment of LRRK2 to stressed lysosomes and induction of LRRK2 kinase activity in response to lysosomal stress (By similarity)

Subunit structure

Forms a conjugate with ATG5 (PubMed:11096062, PubMed:11825910, PubMed:12207896, PubMed:17709747, PubMed:23202584, PubMed:24191030, 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:23202584, PubMed:24191030). Forms an…

Subcellular location

Cytoplasm, Preautophagosomal structure membrane

Experimental structures in the PDB

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

PDB IDMethodResolutionChains and residues
4NAWX-ray2.2 ÅA/E/I/M=52-140
4GDKX-ray2.7 ÅA/D=52-140
4GDLX-ray2.88 ÅA=52-140

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