UniProt A0A0S0VKY7
Outer capsid protein VP4 (A0A0S0VKY7)
Outer capsid protein VP4 (UniProt A0A0S0VKY7): 6 experimental structures on GenesisL1, 4 ligands bound, 3 pockets. Binding sites, pockets, druggability and 3D structures in GL1X.
- UniProt
- A0A0S0VKY7
- Protein
- Outer capsid protein VP4
- Experimental structures
- 6
- Predicted models
- 0
- Ligands
- 4
- Pockets
- 3 · 1 record with a druggable one
Structures
6 records of A0A0S0VKY7 in the MolNFT archive: 6 experimental, 0 predicted.
| Entry | Title | Method | Chains | Ligands | Pockets |
|---|---|---|---|---|---|
| 6H9W | Unraveling the role of the secretor antigen in human rotavirus attachment to histo-blood group… | x-ray diffraction | A | SO4 | — |
| 6H9W | Unraveling the role of the secretor antigen in human rotavirus attachment to histo-blood group… | x-ray diffraction | A | SO4 | — |
| 6H9Z | Molecular bases of histo-blood group antigen recognition by the most common human rotavirus | x-ray diffraction | A, B | SO4 | 3 (best 0.66) |
| 6H9Z | Molecular bases of histo-blood group antigen recognition by the most common human rotavirus | x-ray diffraction | A, B | SO4 | — |
| 6HA0 | Unraveling the role of the secretor antigen in human rotavirus attachment to histo-blood group… | x-ray diffraction | A, B | NAG, GAL, FUC | — |
| 6HA0 | Unraveling the role of the secretor antigen in human rotavirus attachment to histo-blood group… | x-ray diffraction | A, B | NAG, GAL, FUC | — |
Ligands
Elsewhere
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