Research workbench
Cryoem structure of human enterovirus D68 full native virion
Analyse Cryoem structure of human enterovirus D68 full native virion in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6CSG
- Type
- protein
- Length
- 812 residues
- Chains
- 4
- Method
- electron microscopy
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Viral protein 1; Viral protein 3; Viral protein 2; Viral protein 4
- UniProt
- A0A097BW12, A0A1I9KXX3, A0A191Z5D5
- Pockets
- 9 · best druggability 0.70
Structure
electron microscopy · 4 distinct chains · 11% helix, 32% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Viral protein 1 | protein | 289 | 10% helix, 33% strand | A0A097BW12 |
| B | Viral protein 3 | protein | 247 | 9% helix, 30% strand | A0A097BW12 |
| C | Viral protein 2 | protein | 238 | 13% helix, 38% strand | A0A1I9KXX3 |
| D | Viral protein 4 | protein | 38 | 18% helix, 8% strand | A0A191Z5D5 |
Pockets
9 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 254 | 0.70 | 0.85 | 35 | empty |
| 2 | 212 | 0.51 | 0.76 | 33 | empty |
| 3 | 172 | 0.49 | 0.77 | 30 | empty |
| 4 | 131 | 0.44 | 0.77 | 23 | empty |
| 5 | 92 | 0.41 | 0.78 | 21 | empty |
Interfaces
6 interfaces between chains.
- A–B · 4720 Ų buried · 88 hydrogen bonds · protein-protein
- A–C · 2120 Ų buried · 44 hydrogen bonds · protein-protein
- B–C · 1830 Ų buried · 25 hydrogen bonds · protein-protein
- A–D · 1236 Ų buried · 20 hydrogen bonds · protein-protein
- B–D · 934 Ų buried · 13 hydrogen bonds · protein-protein
Compared structures
- 6CSG · CryoEM structure of human enterovirus D68 full native virion · 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 A0A097BW12
- Every structure of UniProt A0A1I9KXX3
- Every structure of UniProt A0A191Z5D5
- Elsewhere: RCSB PDB 6CSG · PDBe 6CSG · UniProt A0A097BW12 · UniProt A0A1I9KXX3 · UniProt A0A191Z5D5
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