ADP-ribosylation factor 6 (ARF6) is a 175-residue protein from Homo sapiens. This is its AlphaFold structure prediction, created 1 Aug 2025. UniProt accession: P62330.
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The mean pLDDT of this model is 94.0 (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 | 88% |
| 70 to 90 | Confident: backbone generally right | 6% |
| 50 to 70 | Low: treat with caution | 5% |
| Below 50 | Very low: often disordered regions | 1% |
What pLDDT means and how to read it
GTP-binding protein involved in protein trafficking that regulates endocytic recycling and cytoskeleton remodeling (PubMed:11266366, PubMed:16737952, PubMed:18400762, PubMed:21170023, PubMed:32103017, PubMed:7589240). GTP-bound form plays an important role in the transport of multiple palmitoylated proteins form the Golgi to the plasma membrane (PubMed:37461827). Required for normal completion of mitotic cytokinesis (By similarity). Plays a role in the reorganization of the actin cytoskeleton and the formation of stress fibers (By similarity). Involved in the regulation of dendritic spine development, contributing to the regulation of dendritic branching and filopodia extension…
Interacts (when activated) with GGA1, GGA2 and GGA3; the interaction is required for proper subcellular location of GGA1, GGA2 and GGA3 (PubMed:11950392). Interacts with PIP5K1C (PubMed:12847086). Interacts with USP6 (via Rab-GAP TBC domain) (PubMed:15509780). Interacts with RAB11FIP3 and RAB11FIP4 (PubMed:16148947, PubMed:17030804, PubMed:17628206). Interacts with HERC1 (PubMed:15642342).…
Cytoplasm, cytosol, Cell membrane, Endosome membrane, Recycling endosome membrane, Cell projection, filopodium membrane, Cell projection, ruffle, Cleavage furrow, Midbody, Midbody ring, Early endosome membrane, Golgi apparatus, trans-Golgi network membrane
Compare the prediction with experimentally determined structures of the same protein:
| PDB ID | Method | Resolution | Chains and residues |
|---|---|---|---|
| 2A5D | X-ray | 1.8 Å | A=1-175 |
| 3N5C | X-ray | 1.82 Å | A/B=14-175 |
| 4KAX | X-ray | 1.85 Å | A=14-173 |
| 2W83 | X-ray | 1.93 Å | A/B/E=13-175 |
| 6PAU | X-ray | 1.93 Å | C=3-9 |
| 2A5F | X-ray | 2.02 Å | A=1-175 |
| 7RK3 | X-ray | 2.05 Å | B=2-9 |
| 1E0S | X-ray | 2.28 Å | A=2-175 |
| 3PCR | X-ray | 2.5 Å | B=14-175 |
| 6PAV | X-ray | 2.52 Å | C=2-9, D=3-9 |
| 2A5G | X-ray | 2.66 Å | A=1-175 |
| 2J5X | X-ray | 2.8 Å | A/B=1-175 |
| 3LVQ | X-ray | 3.38 Å | E=9-175 |
| 3LVR | X-ray | 3.38 Å | E=9-175 |
| 7XRD | EM | 3.9 Å | A/B/C/D=2-175 |
| 4FME | X-ray | 4.1 Å | C/F=14-173 |
| 6BBP | EM | 35.0 Å | A=2-173 |
| 6BBQ | EM | 35.0 Å | A=2-173 |
| 2BAO | NMR | A=2-11 | |
| 2BAU | NMR | A=2-11 |
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