Research workbench
Modeling barmah forest virus structural proteins
Analyse Modeling barmah forest virus structural proteins in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2YEW
- Type
- protein
- Length
- 4,068 residues
- Chains
- 12
- Method
- electron microscopy
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Capsid protein; E1 envelope glycoprotein; E2 envelope glycoprotein
- EC
- 3.4.21.90
- UniProt
- P89946
- Pockets
- 20 · best druggability 0.87
Structure
electron microscopy · 3 distinct chains · 10% helix, 33% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, D, G, J | Capsid protein (EC 3.4.21.90) | protein | 171 | 7% helix, 28% strand | P89946 |
| B, E, H, K | E1 envelope glycoprotein | protein | 425 | 9% helix, 32% strand | P89946 |
| C, F, I, L | E2 envelope glycoprotein | protein | 421 | 13% helix, 38% strand | P89946 |
Pockets
20 pockets found on a 1 Å grid, 17 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 1033 | 0.87 | 0.88 | 112 | empty |
| 2 | 971 | 0.84 | 0.85 | 73 | empty |
| 3 | 1141 | 0.83 | 0.84 | 101 | empty |
| 4 | 1054 | 0.78 | 0.80 | 97 | empty |
| 5 | 764 | 0.73 | 0.79 | 89 | empty |
Interfaces
25 interfaces between chains.
- E–F · 4411 Ų buried · 54 hydrogen bonds · protein-protein
- K–L · 3950 Ų buried · 49 hydrogen bonds · protein-protein
- B–C · 3739 Ų buried · 40 hydrogen bonds · protein-protein
- H–I · 3505 Ų buried · 44 hydrogen bonds · protein-protein
- F–I · 862 Ų buried · 6 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 44 disulfide (disulfide).
Compared structures
- 2YEW · Modeling Barmah Forest virus structural proteins · 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 P89946
- Elsewhere: RCSB PDB 2YEW · PDBe 2YEW · UniProt P89946
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