Research workbench
Pre-fusion state 2 of eeev with localized reconstruction
Analyse Pre-fusion state 2 of eeev with localized reconstruction in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 7N69
- Type
- protein
- Length
- 3,714 residues
- Chains
- 12
- Method
- electron microscopy
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Spike glycoprotein E1; Spike glycoprotein E2
- UniProt
- Q4QXJ7
- Pockets
- 16 · best druggability 0.75
Structure
electron microscopy · 2 distinct chains · 2% helix, 41% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, C, E, G, I, K | Spike glycoprotein E1 | protein | 381 | 3% helix, 41% strand | Q4QXJ7 |
| B, D, F, H, J, L | Spike glycoprotein E2 | protein | 238 | 0% helix, 40% strand | Q4QXJ7 |
Pockets
16 pockets found on a 1 Å grid, 4 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 632 | 0.75 | 0.81 | 80 | empty |
| 2 | 1097 | 0.73 | 0.77 | 83 | empty |
| 3 | 784 | 0.66 | 0.74 | 72 | empty |
| 4 | 299 | 0.58 | 0.78 | 42 | empty |
| 5 | 229 | 0.49 | 0.75 | 25 | empty |
Interfaces
21 interfaces between chains.
- K–L · 2529 Ų buried · 53 hydrogen bonds · protein-protein
- G–H · 2079 Ų buried · 56 hydrogen bonds · protein-protein
- A–B · 1872 Ų buried · 50 hydrogen bonds · protein-protein
- I–J · 1779 Ų buried · 42 hydrogen bonds · protein-protein
- C–D · 1775 Ų buried · 47 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 66 disulfide (disulfide).
Compared structures
- 7N69 · Pre-fusion state 2 of EEEV with localized reconstruction · the same entry in another collection · chain G against G, 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 Q4QXJ7
- Elsewhere: RCSB PDB 7N69 · PDBe 7N69 · UniProt Q4QXJ7
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