Research workbench
Structure of coxsackievirus A10 a-particle
Analyse Structure of coxsackievirus A10 a-particle in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6SNB
- Type
- protein
- Length
- 684 residues
- Chains
- 3
- Method
- electron microscopy
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Capsid protein VP1; Capsid protein VP2; Capsid protein VP3
- EC
- 3.4.22.29, 3.6.1.15, 3.4.22.28, 2.7.7.48
- UniProt
- Q6JKR9
- Pockets
- 9 · best druggability 0.71
Structure
electron microscopy · 3 distinct chains · 9% helix, 31% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Capsid protein VP1 (EC 3.4.22.29, 3.6.1.15, 3.4.22.28, 2.7.7.48) | protein | 223 | 6% helix, 31% strand | Q6JKR9 |
| B | Capsid protein VP2 (EC 3.4.22.29, 3.6.1.15, 3.4.22.28, 2.7.7.48) | protein | 238 | 11% helix, 33% strand | Q6JKR9 |
| C | Capsid protein VP3 (EC 3.4.22.29, 3.6.1.15, 3.4.22.28, 2.7.7.48) | protein | 223 | 9% helix, 30% strand | Q6JKR9 |
Pockets
9 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 297 | 0.71 | 0.84 | 32 | empty |
| 2 | 131 | 0.59 | 0.84 | 22 | empty |
| 3 | 77 | 0.58 | 0.88 | 17 | empty |
| 4 | 76 | 0.48 | 0.82 | 17 | empty |
| 5 | 156 | 0.42 | 0.74 | 28 | empty |
Interfaces
3 interfaces between chains.
- A–C · 3336 Ų buried · 55 hydrogen bonds · protein-protein
- A–B · 1649 Ų buried · 26 hydrogen bonds · protein-protein
- B–C · 1534 Ų buried · 14 hydrogen bonds · protein-protein
Compared structures
- 6SNB · Structure of Coxsackievirus A10 A-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 Q6JKR9
- Elsewhere: RCSB PDB 6SNB · PDBe 6SNB · UniProt Q6JKR9
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