Research workbench
Symmetric reconstruction of human norovirus GII.4 minerva strain vlp in T=4 symmetry
Analyse Symmetric reconstruction of human norovirus GII.4 minerva strain vlp in T=4… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6OUU
- Type
- protein
- Length
- 1,935 residues
- Chains
- 4
- Method
- electron microscopy
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Major capsid protein
- UniProt
- R4I3T2
- Pockets
- 20 · best druggability 0.84
Structure
electron microscopy · 2 distinct chains · 6% helix, 30% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, C, D | Major capsid protein | protein | 485 | 7% helix, 30% strand | R4I3T2 |
| B | Major capsid protein | protein | 480 | 6% helix, 30% strand | R4I3T2 |
Pockets
20 pockets found on a 1 Å grid, 20 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 262 | 0.84 | 0.95 | 44 | empty |
| 2 | 232 | 0.84 | 0.96 | 39 | empty |
| 3 | 220 | 0.83 | 0.95 | 40 | empty |
| 4 | 877 | 0.81 | 0.83 | 91 | empty |
| 5 | 209 | 0.81 | 0.94 | 41 | empty |
Interfaces
5 interfaces between chains.
- C–D · 2221 Ų buried · 26 hydrogen bonds · protein-protein
- B–D · 891 Ų buried · 7 hydrogen bonds · protein-protein
- B–C · 752 Ų buried · 4 hydrogen bonds · protein-protein
- A–B · 659 Ų buried · 0 hydrogen bonds · protein-protein
- A–C · 367 Ų buried · 2 hydrogen bonds · protein-protein
Compared structures
- 6OUU · Symmetric reconstruction of human norovirus GII.4 Minerva strain VLP in T=4 symmetry · the same entry in another collection · chain A against A, TM-score 1.00
Analyse
- Open in the research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides and crosslinks on the 3D structure
- Every structure of UniProt R4I3T2
- Elsewhere: RCSB PDB 6OUU · PDBe 6OUU · UniProt R4I3T2
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