ADP-ribosylation factor-binding protein GGA1 (GGA1) is a 639-residue protein from Homo sapiens. This is its AlphaFold structure prediction, created 1 Aug 2025. UniProt accession: Q9UJY5.
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The mean pLDDT of this model is 73.4 (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 | 45% |
| 70 to 90 | Confident: backbone generally right | 19% |
| 50 to 70 | Low: treat with caution | 7% |
| Below 50 | Very low: often disordered regions | 29% |
What pLDDT means and how to read it
Plays a role in protein sorting and trafficking between the trans-Golgi network (TGN) and endosomes. Mediates the ARF-dependent recruitment of clathrin to the TGN and binds ubiquitinated proteins and membrane cargo molecules with a cytosolic acidic cluster-dileucine (DXXLL) motif (PubMed:11301005, PubMed:15886016). Mediates export of the GPCR receptor ADRA2B to the cell surface (PubMed:27901063). Required for targeting PKD1:PKD2 complex from the trans-Golgi network to the cilium membrane (By similarity). Regulates retrograde transport of proteins such as phosphorylated form of BACE1 from endosomes to the trans-Golgi network (PubMed:15615712, PubMed:15886016)
Monomer (Probable). Interacts with GGA2 and GGA3 (PubMed:14638859). Binds to clathrin and activated ARFs, including ARF1, ARF5 and ARF6 (PubMed:11301005, PubMed:11950392, PubMed:12679809, PubMed:15143060, PubMed:22522702). Interacts with RABEP1 (PubMed:12505986, PubMed:14665628, PubMed:15143060). Interacts with RABGEF1 (PubMed:12505986, PubMed:15143060). Interacts with the type-I membrane…
Golgi apparatus, trans-Golgi network membrane, Endosome membrane, Early endosome membrane
Compare the prediction with experimentally determined structures of the same protein:
| PDB ID | Method | Resolution | Chains and residues |
|---|---|---|---|
| 1J2J | X-ray | 1.6 Å | B=166-210 |
| 3G2S | X-ray | 1.7 Å | A/B=1-147 |
| 1UJK | X-ray | 1.9 Å | A/B=1-147 |
| 1JWG | X-ray | 2.0 Å | A/B=1-147 |
| 3G2T | X-ray | 2.0 Å | A/B=1-147 |
| 1JWF | X-ray | 2.1 Å | A=1-147 |
| 1O3X | X-ray | 2.1 Å | A=166-305 |
| 3G2V | X-ray | 2.1 Å | A/B=1-147 |
| 1NA8 | X-ray | 2.3 Å | A/B=494-639 |
| 2DWY | X-ray | 2.3 Å | A/B/C/D=507-639 |
| 3G2U | X-ray | 2.3 Å | A/B=1-147 |
| 1NWM | X-ray | 2.4 Å | X=166-302 |
| 3G2W | X-ray | 2.4 Å | A/B=1-147, C/D=351-364 |
| 1X79 | X-ray | 2.41 Å | A=210-302 |
| 1OM9 | X-ray | 2.5 Å | A/B=494-639 |
| 2DWX | X-ray | 2.55 Å | A/B/C/D=507-639, P/Q=376-388 |
| 1PY1 | X-ray | 2.6 Å | A/B/C/D=2-157 |
| 1UJJ | X-ray | 2.6 Å | A/B=1-147 |
| 1NAF | X-ray | 2.8 Å | A=165-314 |
| 1OXZ | X-ray | 2.8 Å | A=141-326 |
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