Agnoprotein is a 71-residue protein from JC polyomavirus. This is its AlphaFold structure prediction, created 3 Jul 2025. UniProt accession: P03086.
Explore in 3D Color by confidence AlphaFold DB UniProt
The mean pLDDT of this model is 56.5 (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 | 0% |
| 70 to 90 | Confident: backbone generally right | 18% |
| 50 to 70 | Low: treat with caution | 45% |
| Below 50 | Very low: often disordered regions | 37% |
What pLDDT means and how to read it
Alters the structure of the nuclear envelope by interacting with host CBX5 and disrupting CBX5 association with LBR. Involved in the perinuclear-nuclear localization of the capsid protein VP1 during virion assembly and maturation. Plays an important role in the release of progeny virions from infected cells and in viral propagation, probably by acting as a viral ionic channel in the host plasma membrane. Allows influx of extracellular calcium ions in the host cell. May contribute to viral genome transcription and translation of viral late proteins
Homooligomer. Interacts with VP1 (By similarity). Interacts with large T antigen; this interaction may impact upon the activity of T-antigen on the control of viral gene transcription and replication. Interacts with small t antigen. Interacts with host PP2A subunits for dephosphorylation. Interacts (via N-terminus) with host YBX1; this interaction modulates transcriptional activity genomic…
Host cytoplasm, Host nucleus membrane, Host rough endoplasmic reticulum membrane, Host cell membrane
Compare the prediction with experimentally determined structures of the same protein:
MolViewer loads the AlphaFold model straight from AlphaFold DB into your browser. Show it as a cartoon, color by pLDDT, measure distances and angles, and load a PDB structure next to it to compare.