cGMP-specific 3',5'-cyclic phosphodiesterase (PDE5A) is a 875-residue protein from Homo sapiens. This is its AlphaFold structure prediction, created 1 Aug 2025. UniProt accession: O76074.
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The mean pLDDT of this model is 82.0 (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 | 46% |
| 70 to 90 | Confident: backbone generally right | 35% |
| 50 to 70 | Low: treat with caution | 7% |
| Below 50 | Very low: often disordered regions | 11% |
What pLDDT means and how to read it
Plays a role in signal transduction by regulating the intracellular concentration of cyclic nucleotides. This phosphodiesterase catalyzes the specific hydrolysis of cGMP to 5'-GMP (PubMed:15489334, PubMed:9714779). Specifically regulates nitric-oxide-generated cGMP (PubMed:15489334)
Compare the prediction with experimentally determined structures of the same protein:
| PDB ID | Method | Resolution | Chains and residues |
|---|---|---|---|
| 1TBF | X-ray | 1.3 Å | A=534-858 |
| 1XOZ | X-ray | 1.37 Å | A=534-875 |
| 5JO3 | X-ray | 1.49 Å | B=534-858 |
| 2CHM | X-ray | 1.6 Å | A=534-657, A=683-858 |
| 1XP0 | X-ray | 1.79 Å | A=534-875 |
| 3HC8 | X-ray | 1.79 Å | A=536-657, A=683-858 |
| 2H44 | X-ray | 1.8 Å | A=535-860 |
| 3HDZ | X-ray | 1.8 Å | A=536-657, A=683-858 |
| 2H40 | X-ray | 1.85 Å | A=535-860 |
| 8W4S | X-ray | 1.85 Å | A=535-860 |
| 3TGG | X-ray | 1.91 Å | A=534-858 |
| 6L6E | X-ray | 1.92 Å | A=536-861 |
| 3SIE | X-ray | 1.93 Å | A/B=535-860 |
| 3TGE | X-ray | 1.96 Å | A=534-858 |
| 1T9S | X-ray | 2.0 Å | A/B=534-858 |
| 3BJC | X-ray | 2.0 Å | A=1-875 |
| 4MD6 | X-ray | 2.0 Å | A=535-860 |
| 1RKP | X-ray | 2.05 Å | A=535-860 |
| 3B2R | X-ray | 2.07 Å | A/B=535-860 |
| 4I9Z | X-ray | 2.08 Å | A=535-860 |
Showing 20 of 50 experimental structures (best resolution first).
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