AP-1 complex subunit gamma-1 (Ap1g1) is a 822-residue protein from Mus musculus. This is its AlphaFold structure prediction, created 1 Aug 2025. UniProt accession: P22892.
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The mean pLDDT of this model is 83.0 (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 | 64% |
| 70 to 90 | Confident: backbone generally right | 21% |
| 50 to 70 | Low: treat with caution | 1% |
| Below 50 | Very low: often disordered regions | 14% |
What pLDDT means and how to read it
Subunit of clathrin-associated adaptor protein complex 1 that plays a role in protein sorting in the late-Golgi/trans-Golgi network (TGN) and/or endosomes (PubMed:36261523). The AP complexes mediate both the recruitment of clathrin to membranes and the recognition of sorting signals within the cytosolic tails of transmembrane cargo molecules (PubMed:36261523). In association with AFTPH/aftiphilin in the aftiphilin/p200/gamma-synergin complex, involved in the trafficking of transferrin from early to recycling endosomes, and the membrane trafficking of furin and the lysosomal enzyme cathepsin D between the trans-Golgi network (TGN) and endosomes (By similarity)
Adaptor protein complex 1 (AP-1) is a heterotetramer composed of two large adaptins (gamma-type subunit AP1G1 and beta-type subunit AP1B1), a medium adaptin (mu-type subunit AP1M1 or AP1M2) and a small adaptin (sigma-type subunit AP1S1 or AP1S2 or AP1S3) (PubMed:36261523). Interacts (via GAE domain) with RABEP1 (By similarity). Interacts with EPS15 (PubMed:12176391). Interacts with…
Golgi apparatus, Cytoplasmic vesicle, clathrin-coated vesicle membrane, Cytoplasm, Cytoplasm, perinuclear region, Cytoplasmic vesicle, clathrin-coated vesicle, Membrane, clathrin-coated pit
Compare the prediction with experimentally determined structures of the same protein:
| PDB ID | Method | Resolution | Chains and residues |
|---|---|---|---|
| 3ZY7 | X-ray | 1.09 Å | A/B=704-822 |
| 2A7B | X-ray | 1.65 Å | A=704-822 |
| 1GYV | X-ray | 1.71 Å | A=704-822 |
| 1GYU | X-ray | 1.81 Å | A=704-822 |
| 7R4H | EM | 2.34 Å | G=1-595 |
| 1GYW | X-ray | 2.4 Å | A/B=695-822 |
| 4P6Z | X-ray | 3.0 Å | G=1-613 |
| 6CM9 | EM | 3.73 Å | G=1-595 |
| 6DFF | EM | 3.9 Å | G=1-595 |
| 1W63 | X-ray | 4.0 Å | A/C/E/G/I/K=1-613 |
| 6D83 | EM | 4.27 Å | G=1-595 |
| 6D84 | EM | 6.72 Å | G/K=1-595 |
| 6CRI | EM | 6.8 Å | G/Q/R=4-588 |
| 4HMY | X-ray | 7.0 Å | A=1-595 |
| 8D4E | EM | 9.2 Å | G=1-595 |
| 8D4C | EM | 9.3 Å | E/G=2-595 |
| 8D9W | EM | 9.3 Å | K/O=1-595 |
| 8D9V | EM | 9.4 Å | E/G=1-595 |
| 7UX3 | EM | 9.6 Å | G=2-595 |
| 8D4D | EM | 9.6 Å | E/G=1-595 |
Showing 20 of 26 experimental structures (best resolution first).
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