Research workbench
Pre-fusion state 1 of eeev with localized reconstruction
Analyse Pre-fusion state 1 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
- 7N6A
- Type
- protein
- Length
- 4,506 residues
- Chains
- 12
- Method
- electron microscopy
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Spike glycoprotein E1; Spike glycoprotein E2
- UniProt
- Q4QXJ7
- Pockets
- 12 · best druggability 0.76
Structure
electron microscopy · 2 distinct chains · 1% helix, 28% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, C, E, G, I, K | Spike glycoprotein E1 | protein | 400 | 1% helix, 28% strand | Q4QXJ7 |
| B, D, F, H, J, L | Spike glycoprotein E2 | protein | 351 | 2% helix, 28% strand | Q4QXJ7 |
Pockets
12 pockets found on a 1 Å grid, 4 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 818 | 0.76 | 0.80 | 105 | empty |
| 2 | 645 | 0.69 | 0.78 | 75 | empty |
| 3 | 456 | 0.66 | 0.79 | 45 | empty |
| 4 | 392 | 0.59 | 0.76 | 53 | empty |
| 5 | 164 | 0.49 | 0.77 | 20 | empty |
Interfaces
23 interfaces between chains.
- G–H · 4706 Ų buried · 146 hydrogen bonds · protein-protein
- E–F · 4683 Ų buried · 147 hydrogen bonds · protein-protein
- I–J · 4648 Ų buried · 140 hydrogen bonds · protein-protein
- K–L · 4572 Ų buried · 126 hydrogen bonds · protein-protein
- A–B · 4385 Ų buried · 146 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 84 disulfide (disulfide).
Compared structures
- 7N6A · Pre-fusion state 1 of EEEV with localized reconstruction · 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 Q4QXJ7
- Elsewhere: RCSB PDB 7N6A · PDBe 7N6A · UniProt Q4QXJ7
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