Golgi-associated PDZ and coiled-coil motif-containing protein (GOPC) is a 462-residue protein from Homo sapiens. This is its AlphaFold structure prediction, created 1 Aug 2025. UniProt accession: Q9HD26.
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The mean pLDDT of this model is 69.1 (low 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 | 22% |
| 70 to 90 | Confident: backbone generally right | 35% |
| 50 to 70 | Low: treat with caution | 19% |
| Below 50 | Very low: often disordered regions | 24% |
What pLDDT means and how to read it
Plays a role in intracellular protein trafficking and degradation (PubMed:11707463, PubMed:14570915, PubMed:15358775). May regulate CFTR chloride currents and acid-induced ASIC3 currents by modulating cell surface expression of both channels (By similarity). May also regulate the intracellular trafficking of the ADR1B receptor (PubMed:15358775). May play a role in autophagy (By similarity). Together with MARCHF2 mediates the ubiquitination and lysosomal degradation of CFTR (PubMed:23818989). Overexpression results in CFTR intracellular retention and lysosomaldegradation in the lysosomes (PubMed:11707463, PubMed:14570915)
Homooligomer (By similarity). Interacts with FZD5 (By similarity). Interacts with FZD8 (PubMed:16882988). Interacts with GRID2 and BECN1 (By similarity). Interacts with CSPG5 (By similarity). Interacts with CLCN3 (By similarity). Interacts with STX6 (PubMed:11384996). Interacts with CFTR (PubMed:11707463). Interacts with ASIC3 (PubMed:15317815). Interacts with GOLGA3 (PubMed:15951434). Interacts…
Cytoplasm, Golgi apparatus membrane, Golgi apparatus, trans-Golgi network membrane, Synapse, Postsynaptic density, Cell projection, dendrite
Compare the prediction with experimentally determined structures of the same protein:
| PDB ID | Method | Resolution | Chains and residues |
|---|---|---|---|
| 4JOK | X-ray | 1.09 Å | A/B=284-370 |
| 4JOE | X-ray | 1.14 Å | A/B=284-370 |
| 4JOF | X-ray | 1.2 Å | A/B=284-370 |
| 4JOJ | X-ray | 1.2 Å | A/B=284-370 |
| 4NMP | X-ray | 1.3 Å | A/B=284-370 |
| 4JOR | X-ray | 1.34 Å | A/B=284-370 |
| 7JZQ | X-ray | 1.35 Å | A=284-370 |
| 5K4F | X-ray | 1.36 Å | A/B=284-370 |
| 4E34 | X-ray | 1.4 Å | A/B=284-370 |
| 4E35 | X-ray | 1.4 Å | A/B=284-370 |
| 4NMO | X-ray | 1.4 Å | A/B=284-370 |
| 4NMQ | X-ray | 1.4 Å | A/B=284-370 |
| 4NMT | X-ray | 1.4 Å | A/B=284-370 |
| 4NMV | X-ray | 1.4 Å | A/B=284-370 |
| 4Q6S | X-ray | 1.45 Å | A/B=284-370 |
| 4JOG | X-ray | 1.46 Å | A/B=284-370 |
| 4JOH | X-ray | 1.47 Å | A/B=284-370 |
| 4K6Y | X-ray | 1.48 Å | A/B=284-370 |
| 4K75 | X-ray | 1.5 Å | A=284-370 |
| 7JZR | X-ray | 1.54 Å | A/B=284-370 |
Showing 20 of 35 experimental structures (best resolution first).
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