E3 ubiquitin-protein ligase COP1 (COP1) is a 675-residue protein from Arabidopsis thaliana. This is its AlphaFold structure prediction, created 1 Aug 2025. UniProt accession: P43254.
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The mean pLDDT of this model is 80.1 (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 | 57% |
| 70 to 90 | Confident: backbone generally right | 17% |
| 50 to 70 | Low: treat with caution | 9% |
| Below 50 | Very low: often disordered regions | 17% |
What pLDDT means and how to read it
E3 ubiquitin-protein ligase that acts as a repressor of photomorphogenesis and as an activator of etiolation in darkness. E3 ubiquitin ligases accept ubiquitin from an E2 ubiquitin-conjugating enzyme in the form of a thioester and then directly transfers the ubiquitin to targeted substrates. Represses photomorphogenesis in darkness by mediating ubiquitination and subsequent proteasomal degradation of light-induced transcription factors such as HY5, HYH and LAF1. Down-regulates MYB21, probably via ubiquitination process. Light stimuli abrogate the repression of photomorphogenesis, possibly due to its localization to the cytoplasm. Could play a role in switching between skotomorphogenetic…
Homodimer. Interacts with HY5, HYH, BBX24/STO, BBX25/STH, CIP8, COP10, SPA1, SPA2, SPA3, SPA4 and UVR8 and phosphorylated PHYA. Light induces dissociation of the SPA1/COP1 complex. Interacts with HRT/RPP8 and triggers it to the 26s proteasome. Binds to CRY2; this competitive interaction prevents triggering to proteasome of other binding proteins (PubMed:20624951). Binds to SHW1 in the nucleus…
Nucleus, Cytoplasm
Compare the prediction with experimentally determined structures of the same protein:
| PDB ID | Method | Resolution | Chains and residues |
|---|---|---|---|
| 6QTS | X-ray | 1.11 Å | A=349-675 |
| 6QTO | X-ray | 1.27 Å | A=349-675 |
| 6QTQ | X-ray | 1.3 Å | A=349-675 |
| 6QTU | X-ray | 1.3 Å | A=349-675 |
| 6QTV | X-ray | 1.31 Å | A=349-675 |
| 6QTR | X-ray | 1.37 Å | A=349-675 |
| 6QTW | X-ray | 1.39 Å | A=349-675 |
| 5KWN | X-ray | 1.42 Å | A=349-675 |
| 6QTT | X-ray | 1.51 Å | A=349-675 |
| 5IGO | X-ray | 1.6 Å | A/B/C/D=349-675 |
| 6QTX | X-ray | 1.95 Å | A=349-675 |
| 7VGG | EM | 3.1 Å | A=1-675 |
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