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Prediction Confidence (pLDDT)

Very low pLDDT < 50

Low 50 < pLDDT < 70

High 70 < pLDDT < 90

Very high pLDDT > 90

Very low Low High Very high

Tap a block to see the pLDDT value corresponding to its color

Cartoon Surface

Quality:

Medium Lower Lowest

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Confidence Chain

This coat protein structural model was generated using AlphaFold2.

FoldaVirus Score

Anomaly

Good Best

0 2.72

Structure View

IAU Capsid

General Information

UniProtKB:
Taxonomy ID:

Genus:
T-Number:
Diameter:	-- min -- avg -- max
Ref. Structure
-- TM-score -- RMSD -- Identity -- Similarity -- Aln. Length

VIPER Analysis & Annotations

Mahalanobis Analysis Anomaly Detection Tool Accessible Surface Profile Association Energies Contacts Table Capsid Explorer NEW

Residue Annotations Analysis

Mahalanobis Plot

Threshold (at --% confidence level) --

Mahalanobis Distance (MD)

Prediction MD --

Reference (--) MD --

Prediction ↔ Reference MD --

FoldaVirus Score --

The Foldavirus Score is estimated as

Foldavirus Score = max( Threshold − Prediction MD, Threshold − MD between Prediction and Reference )

Surface Profile Analysis

Surface Profiles:

Download CSV

Energy Analysis

Interface	Symmetry	Association Energy (Kcal/mol)	Buried Surface Area (Å)	Solvation Energy (Kcal/mol)	Relative Strength (% BSA)

Important Considerations

The association and solvation energies shown in the table above were calculated based on buried surface areas and atomic solvation parameters. We strongly believe that the relative energies (i.e., strengths of the interfaces) are reflected in these numbers. Use them with caution when comparing with experimental values.

References

Reddy, V. S., Giesing, H. A., Morton, R. T., Kumar, A., Post, C. B., Brooks, C. L., 3rd, & Johnson, J. E. (1998). "Energetics of quasiequivalence: computational analysis of protein-protein interactions in icosahedral viruses."
Biophysical Journal, 74(1), 546–558. PMID: 9449355
Horton, N., & Lewis, M. (1992). "Calculation of the free energy of association for protein complexes."
Protein Science, 1(1), 169–181. PMID: 1339024
Eisenberg, D., & McLachlan, A. D. (1986). "Solvation energy in protein folding and binding."
Nature, 319(6050), 199–203. PMID: 3945310

Residue Types:

A Acidic

B Basic

H Hydrophobic

NA Nucleic Acid

P Polar, uncharged

Individual Contacts

Download data

Contacts by Interface

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Highly accurate protein structure prediction with AlphaFold Jumper, J., Evans, R., Pritzel, A., et al. Nature 596, 583–589 (2021). 10.1038/s41586-021-03819-2

Protein complex prediction with AlphaFold-Multimer Evans, R., O'Neill, M., Pritzel, A., et al. bioRxiv (2021). 10.1101/2021.10.04.463034

Accurate structure prediction of biomolecular interactions with AlphaFold 3 Abramson, J., et al. Nature 630, 493–500 (2024). 10.1038/s41586-024-07487-w

Prediction Confidence (pLDDT)

Model Attributes

Structure View

General Information

VIPER Analysis & Annotations

Analysis Details

Residue Annotations Analysis

Mahalanobis Plot

Surface Profile Analysis

Energy Analysis

Important Considerations

References

Individual Contacts

Contacts by Interface

Capsid Explorer

Structure Details

Residue Annotations

Find Residues

References

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