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Structure of the st. louis encephalitis virus envelope protein in the fusogenic trimer conformation.
Analyse Structure of the st. louis encephalitis virus envelope protein in the fusogenic… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 4FG0
- Type
- protein
- Length
- 386 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Polyprotein
- UniProt
- Q9ENF3
- Pockets
- 3 · best druggability 0.52
Structure
x-ray diffraction · 1 distinct chain · 6% helix, 48% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Polyprotein | protein | 386 | 6% helix, 48% strand | Q9ENF3 |
Pockets
3 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 195 | 0.52 | 0.77 | 34 | empty |
| 2 | 100 | 0.46 | 0.80 | 22 | empty |
| 3 | 135 | 0.42 | 0.75 | 25 | empty |
Modifications
Observed in the structure: 7 modified, 6 disulfide (engineered, disulfide).
Compared structures
- 4FG0 · Structure of the St. Louis Encephalitis Virus envelope protein in the fusogenic trimer… · 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 Q9ENF3
- Elsewhere: RCSB PDB 4FG0 · PDBe 4FG0 · UniProt Q9ENF3
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