UniProt P26747
Major capsid protein (P26747)
Major capsid protein (UniProt P26747): 10 experimental structures on GenesisL1, 60 pockets. Binding sites, pockets, druggability and 3D structures in GL1X.
- UniProt
- P26747
- Protein
- Major capsid protein
- Experimental structures
- 10
- Predicted models
- 0
- Pockets
- 60 · 3 records with a druggable one
Structures
10 records of P26747 in the MolNFT archive: 10 experimental, 0 predicted.
| Entry | Title | Method | Chains | Ligands | Pockets |
|---|---|---|---|---|---|
| 2M5S | High-resolution NMR structure and cryo-EM imaging support multiple functional roles for the… | solution nmr | A | — | — |
| 2M5S | High-resolution NMR structure and cryo-EM imaging support multiple functional roles for the… | solution nmr | A | — | — |
| 3IYH | P22 procapsid coat protein structures reveal a novel mechanism for capsid maturation: Stability… | electron microscopy | A, B, C, D, E, F | — | — |
| 3IYH | P22 procapsid coat protein structures reveal a novel mechanism for capsid maturation: stability… | electron microscopy | A, B, C, D, E, F | — | — |
| 3IYI | P22 expanded head coat protein structures reveal a novel mechanism for capsid maturation: Stability… | electron microscopy | A, B, C, D, E, F, G | — | — |
| 3IYI | P22 expanded head coat protein structures reveal a novel mechanism for capsid maturation: stability… | electron microscopy | A, B, C, D, E, F, G | — | — |
| 5UU5 | Bacteriophage P22 mature virion capsid protein | electron microscopy | G, A, C, E, F, B, D | — | 20 (best 0.83) |
| 5UU5 | Bacteriophage P22 mature virion capsid protein | electron microscopy | G, A, C, E, F, B, D | — | — |
| 8GN5 | Designed pH-responsive P22 VLP | electron microscopy | A, B, C, D | — | 20 (best 0.83) |
| 8I1T | The asymmetric unit of P22 empty capsid | electron microscopy | G, A, C, E, F, B, D | — | 20 (best 0.82) |
Elsewhere
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