Research workbench
The structure of rhinovirus 16
Analyse The structure of rhinovirus 16 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1ND2
- Type
- protein
- Length
- 804 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Coat protein VP1; Coat protein VP2; Coat protein VP3; Coat protein VP4
- UniProt
- Q82122
- Ligands
- MYR, ZN
- Pockets
- 14 · best druggability 0.80
Structure
x-ray diffraction · 4 distinct chains · 12% helix, 32% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Coat protein VP1 | protein | 285 | 14% helix, 32% strand | Q82122 |
| B | Coat protein VP2 | protein | 252 | 13% helix, 37% strand | Q82122 |
| C | Coat protein VP3 | protein | 238 | 9% helix, 31% strand | Q82122 |
| D | Coat protein VP4 | protein | 29 | 10% helix, 21% strand | Q82122 |
Ligands and binding sites
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
14 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 213 | 0.80 | 0.93 | 38 | MYR |
| 2 | 326 | 0.55 | 0.75 | 44 | empty |
| 3 | 200 | 0.50 | 0.76 | 22 | empty |
| 4 | 108 | 0.49 | 0.80 | 21 | empty |
| 5 | 150 | 0.45 | 0.76 | 32 | empty |
Interfaces
5 interfaces between chains.
- A–C · 4243 Ų buried · 65 hydrogen bonds · protein-protein
- A–B · 2090 Ų buried · 43 hydrogen bonds · protein-protein
- B–C · 1671 Ų buried · 20 hydrogen bonds · protein-protein
- A–D · 676 Ų buried · 8 hydrogen bonds · protein-protein
- C–D · 369 Ų buried · 6 hydrogen bonds · protein-protein
Compared structures
- 1ND2 · The structure of Rhinovirus 16 · 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 Q82122
- Elsewhere: RCSB PDB 1ND2 · PDBe 1ND2 · UniProt Q82122
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