MolNFT v1 · #91530 · protein
Structure of the st. louis encephalitis virus envelope protein in the fusogenic trimer conformation.
4FG0 · Polyprotein: “Structure of the st. louis encephalitis virus envelope protein in the fusogenic trimer conformation.”. X-ray diffraction, 3 pockets (best druggability 0.52). MolNFT v1 #91530 on GenesisL1: 3D structure, binding sites…
- 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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