Gamma-aminobutyric acid receptor-associated protein (GABARAP) is a 117-residue protein from Homo sapiens. This is its AlphaFold structure prediction, created 1 Aug 2025. UniProt accession: O95166.
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The mean pLDDT of this model is 94.9 (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 band | Meaning | Share of residues |
|---|---|---|
| Above 90 | Very high: backbone and side chains are usually accurate | 91% |
| 70 to 90 | Confident: backbone generally right | 8% |
| 50 to 70 | Low: treat with caution | 2% |
| Below 50 | Very low: often disordered regions | 0% |
What pLDDT means and how to read it
Ubiquitin-like modifier that plays a role in intracellular transport of GABA(A) receptors and its interaction with the cytoskeleton (PubMed:9892355). Involved in autophagy: while LC3s are involved in elongation of the phagophore membrane, the GABARAP/GATE-16 subfamily is essential for a later stage in autophagosome maturation (PubMed:15169837, PubMed:20562859, PubMed:22948227, PubMed:34597140). Through its interaction with the reticulophagy receptor TEX264, participates in the remodeling of subdomains of the endoplasmic reticulum into autophagosomes upon nutrient stress, which then fuse with lysosomes for endoplasmic reticulum turnover (PubMed:31006538). Participates in selective ER-phagy…
Interacts with GPHN and NSF (By similarity). Interacts with ATG7, ATG13 (PubMed:11096062, PubMed:12507496, PubMed:23043107). Interacts with ATG3 (PubMed:11825910, PubMed:12507496, PubMed:37252361). Interacts with alpha- and beta-tubulin (PubMed:11729197, PubMed:9892355). Interacts with GABRG2 (PubMed:11729197, PubMed:9892355). Interacts with RB1CC1 (PubMed:23043107). Interacts with ULK1…
Cytoplasmic vesicle, autophagosome membrane, Endomembrane system, Cytoplasm, cytoskeleton, Golgi apparatus membrane, Cytoplasmic vesicle
Compare the prediction with experimentally determined structures of the same protein:
| PDB ID | Method | Resolution | Chains and residues |
|---|---|---|---|
| 6HYO | X-ray | 1.07 Å | A=1-117 |
| 6YOP | X-ray | 1.1 Å | A=1-117 |
| 7ZKR | X-ray | 1.1 Å | A=1-117 |
| 6HYN | X-ray | 1.14 Å | A=1-117 |
| 7AA8 | X-ray | 1.25 Å | C=1-117 |
| 6HOG | X-ray | 1.26 Å | A=2-112 |
| 8T2M | X-ray | 1.27 Å | A=1-117 |
| 3D32 | X-ray | 1.3 Å | A/B=1-117 |
| 6HB9 | X-ray | 1.3 Å | A=3-116 |
| 7BRQ | X-ray | 1.4 Å | A=1-116 |
| 9I9X | X-ray | 1.42 Å | A=1-117 |
| 9HGD | X-ray | 1.5 Å | A/C=1-117 |
| 6HOJ | X-ray | 1.51 Å | A/B/C=1-112 |
| 8W6A | X-ray | 1.53 Å | A/B/D/G=1-117 |
| 7ZL7 | X-ray | 1.55 Å | A/C=1-117 |
| 6HYL | X-ray | 1.56 Å | A/B=1-117 |
| 8T33 | X-ray | 1.6 Å | A=1-117 |
| 6HOK | X-ray | 1.61 Å | A=1-112 |
| 1GNU | X-ray | 1.75 Å | A=1-117 |
| 7YO9 | X-ray | 1.75 Å | A=1-116 |
Showing 20 of 43 experimental structures (best resolution first).
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