Oplophorus-luciferin 2-monooxygenase catalytic subunit is a 196-residue protein from Oplophorus gracilirostris. This is its AlphaFold structure prediction, created 1 Aug 2025. UniProt accession: Q9GV45.
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The mean pLDDT of this model is 84.7 (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 | 24% |
| 50 to 70 | Low: treat with caution | 6% |
| Below 50 | Very low: often disordered regions | 12% |
What pLDDT means and how to read it
Catalytic subunit of oplophorus-luciferin 2-monooxygenase. Oxidoreductase that converts coelenterazine (the oplophorus luciferin) to coelenteramide under emission of blue light with a maximum at 454 nm. Is also active with bisdeoxycoelenterazine
Heterotetramer of a catalytic 19 kDa and a non-catalytic 35 kDa subunit
Secreted
Compare the prediction with experimentally determined structures of the same protein:
| PDB ID | Method | Resolution | Chains and residues |
|---|---|---|---|
| 7SNS | X-ray | 1.55 Å | A/B/C/D=28-196 |
| 8AQ6 | X-ray | 1.69 Å | A/B/C/D/E/F/G/H=28-196 |
| 7SNX | X-ray | 1.7 Å | A=28-183, B=185-195 |
| 7VSX | X-ray | 1.7 Å | A=28-196 |
| 5B0U | X-ray | 1.71 Å | A/B=28-196 |
| 7SNW | X-ray | 1.8 Å | A/B/C=28-196 |
| 5IBO | X-ray | 1.95 Å | A/B=28-196 |
| 8AQI | X-ray | 1.99 Å | A/B/C/D/E/F/G/H=28-196 |
| 7SNR | X-ray | 2.0 Å | A/B=28-196 |
| 7SNY | X-ray | 2.1 Å | A=28-183 |
| 7SNT | X-ray | 2.2 Å | A/B=28-196 |
| 9UPV | EM | 2.7 Å | R=32-183 |
| 8AQH | X-ray | 2.8 Å | A/B=28-196 |
| 9UPU | EM | 2.8 Å | R=32-183 |
| 9K07 | EM | 2.83 Å | R=28-183 |
| 8JPN | EM | 2.9 Å | R=28-184 |
| 9LWP | EM | 2.93 Å | R=28-183 |
| 8HNM | EM | 2.94 Å | R=27-184 |
| 8HNL | EM | 2.98 Å | R=27-184 |
| 8HCQ | EM | 3.01 Å | R=11-184 |
Showing 20 of 24 experimental structures (best resolution first).
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