Research workbench
Cryoem structure of human enterovirus 70 native virion
Analyse Cryoem structure of human enterovirus 70 native virion in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 7OPX
- Type
- protein
- Length
- 810 residues
- Chains
- 4
- Method
- electron microscopy
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Capsid protein VP1; Capsid protein VP2; Capsid protein VP3; Capsid protein VP4
- UniProt
- P32537
- Pockets
- 11 · best druggability 0.75
Structure
electron microscopy · 4 distinct chains · 10% helix, 32% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Capsid protein VP1 | protein | 297 | 10% helix, 30% strand | P32537 |
| B | Capsid protein VP2 | protein | 238 | 13% helix, 39% strand | P32537 |
| C | Capsid protein VP3 | protein | 243 | 6% helix, 31% strand | P32537 |
| D | Capsid protein VP4 | protein | 32 | 22% helix, 9% strand | P32537 |
Pockets
11 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 329 | 0.75 | 0.86 | 50 | empty |
| 2 | 218 | 0.54 | 0.78 | 35 | empty |
| 3 | 88 | 0.47 | 0.82 | 21 | empty |
| 4 | 171 | 0.46 | 0.75 | 30 | empty |
| 5 | 124 | 0.44 | 0.77 | 22 | empty |
Interfaces
6 interfaces between chains.
- A–C · 4515 Ų buried · 73 hydrogen bonds · protein-protein
- A–B · 2052 Ų buried · 41 hydrogen bonds · protein-protein
- B–C · 1727 Ų buried · 20 hydrogen bonds · protein-protein
- A–D · 854 Ų buried · 12 hydrogen bonds · protein-protein
- C–D · 833 Ų buried · 8 hydrogen bonds · protein-protein
Compared structures
- 7OPX · CryoEM structure of human enterovirus 70 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 P32537
- Elsewhere: RCSB PDB 7OPX · PDBe 7OPX · UniProt P32537
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