ADP-ribosylation factor 1 (ARF1) is a 181-residue protein from Homo sapiens. This is its AlphaFold structure prediction, created 1 Aug 2025. UniProt accession: P84077.
Explore in 3D Color by confidence AlphaFold DB UniProt
The mean pLDDT of this model is 85.9 (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 band | Meaning | Share of residues |
|---|---|---|
| Above 90 | Very high: backbone and side chains are usually accurate | 58% |
| 70 to 90 | Confident: backbone generally right | 26% |
| 50 to 70 | Low: treat with caution | 11% |
| Below 50 | Very low: often disordered regions | 5% |
What pLDDT means and how to read it
Small GTPase involved in protein trafficking between different compartments (PubMed:8253837). Modulates vesicle budding and uncoating within the Golgi complex (PubMed:8253837). In its GTP-bound form, triggers the recruitment of coatomer proteins to the Golgi membrane (PubMed:8253837). The hydrolysis of ARF1-bound GTP, which is mediated by ARFGAPs proteins, is required for dissociation of coat proteins from Golgi membranes and vesicles (PubMed:8253837). The GTP-bound form interacts with PICK1 to limit PICK1-mediated inhibition of Arp2/3 complex activity; the function is linked to AMPA receptor (AMPAR) trafficking, regulation of synaptic plasticity of excitatory synapses and spine shrinkage…
Interacts (when activated) with GGA1, GGA2 and GGA3; the interaction is required for proper subcellular location of GGA1, GGA2 and GGA3 (PubMed:11950392, PubMed:28868155). Interacts with ARHGAP21, ASAP2, HERC1, PRKCABP, PIP5K1B, TMED2, PSCD2, TMED10 and GRIA2 (PubMed:10022920, PubMed:17347647, PubMed:23889934, PubMed:8861955). Interacts with ARFGAP1, which hydrolyzes GTP and thus, regulates its…
Golgi apparatus membrane, Synapse, synaptosome, Postsynaptic density
Compare the prediction with experimentally determined structures of the same protein:
| PDB ID | Method | Resolution | Chains and residues |
|---|---|---|---|
| 8SDW | X-ray | 1.75 Å | A=1-181 |
| 1HUR | X-ray | 2.0 Å | A/B=2-181 |
| 7R4H | EM | 2.34 Å | C/H=17-181 |
| 6FAE | X-ray | 2.35 Å | B=18-181 |
| 1RE0 | X-ray | 2.4 Å | A=18-181 |
| 9QLO | EM | 2.47 Å | CZ=2-181 |
| 9QLQ | EM | 2.57 Å | CZ=2-181 |
| 7DN8 | X-ray | 2.61 Å | B/D/F/H=17-181 |
| 9QLP | EM | 2.75 Å | CZ=2-181 |
| 3O47 | X-ray | 2.8 Å | A/B=11-181 |
| 7DN9 | X-ray | 3.29 Å | B/D/F/H=17-181 |
| 6CM9 | EM | 3.73 Å | C/H=17-181 |
| 6DFF | EM | 3.9 Å | C/H=17-181 |
| 7MGE | EM | 3.94 Å | E=17-180 |
| 9C5A | EM | 4.2 Å | C/c=2-181 |
| 6D83 | EM | 4.27 Å | C/H=17-181 |
| 9C59 | EM | 4.3 Å | A/C/a/c=2-181 |
| 9C5B | EM | 4.5 Å | A/C=2-181 |
| 9C58 | EM | 4.7 Å | A=2-181 |
| 6D84 | EM | 6.72 Å | C/H/I/N=17-181 |
Showing 20 of 34 experimental structures (best resolution first).
MolViewer loads the AlphaFold model straight from AlphaFold DB into your browser. Show it as a cartoon, color by pLDDT, measure distances and angles, and load a PDB structure next to it to compare.