Research workbench
Crystal structure of empty human enterovirus 71 particle
Analyse Crystal structure of empty human enterovirus 71 particle in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3VBU
- Type
- protein
- Length
- 694 residues
- Chains
- 3
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Genome polyprotein, capsid protein VP1; Genome polyprotein, capsid protein VP0; Genome…
- UniProt
- B2ZUN0
- Pockets
- 8 · best druggability 0.66
Structure
x-ray diffraction · 3 distinct chains · 9% helix, 35% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Genome polyprotein, capsid protein VP1 | protein | 218 | 7% helix, 33% strand | B2ZUN0 |
| B | Genome polyprotein, capsid protein VP0 | protein | 237 | 8% helix, 38% strand | B2ZUN0 |
| C | Genome polyprotein, capsid protein VP3 | protein | 239 | 10% helix, 35% strand | B2ZUN0 |
Pockets
8 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 317 | 0.66 | 0.81 | 34 | empty |
| 2 | 260 | 0.53 | 0.76 | 33 | empty |
| 3 | 121 | 0.49 | 0.80 | 25 | empty |
| 4 | 160 | 0.46 | 0.76 | 35 | empty |
| 5 | 76 | 0.40 | 0.79 | 19 | empty |
Interfaces
3 interfaces between chains.
- A–C · 3103 Ų buried · 50 hydrogen bonds · protein-protein
- A–B · 1823 Ų buried · 30 hydrogen bonds · protein-protein
- B–C · 1560 Ų buried · 19 hydrogen bonds · protein-protein
Compared structures
- 3VBU · Crystal structure of empty human Enterovirus 71 particle · 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 B2ZUN0
- Elsewhere: RCSB PDB 3VBU · PDBe 3VBU · UniProt B2ZUN0
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