4GQH
The Conformations and Interactions of the Four-Layer Aggregate Revealed by X-ray Crystallography Diffraction Implied the Importance of Peptides at Opposite Ends in Their Assemblies
Summary for 4GQH
Entry DOI | 10.2210/pdb4gqh/pdb |
Descriptor | Capsid protein (1 entity in total) |
Functional Keywords | hydrogen-bonding, the four-layer aggregate, viral protein |
Biological source | Tobacco mosaic virus (TMV) |
Cellular location | Virion (Potential): P69687 |
Total number of polymer chains | 34 |
Total formula weight | 657915.40 |
Authors | Li, X.Y.,Song, B.A.,Hu, D.Y.,Chen, X.,Wang, Z.C.,Zeng, M.J.,Yu, D.D.,Chen, Z.,Jin, L.H.,Yang, S. (deposition date: 2012-08-23, release date: 2013-08-28, Last modification date: 2024-03-20) |
Primary citation | Li, X.Y.,Song, B.A.,Hu, D.Y.,Chen, X.,Wang, Z.C.,Zeng, M.J.,Yu, D.D.,Chen, Z.,Jin, L.H.,Yang, S. The Conformations and Interactions of the Four-Layer Aggregate Revealed by X-ray Crystallography Diffraction Implied the Importance of Peptides at Opposite Ends in Their Assemblies To be Published, |
Experimental method | X-RAY DIFFRACTION (3.06 Å) |
Structure validation
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