Research workbench
Three-dimensional structures of drug-resistant mutants of human rhinovirus 14
Analyse Three-dimensional structures of drug-resistant mutants of human rhinovirus 14 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2RMU
- Type
- protein
- Length
- 804 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v2 / PDB Bank
- Contract
- 0xd58B01f6C18086e5202cdC5D7Ad3E41790360102
- Owner
- 0xF4e1AA6f26B7DA48EeAD9B24a97927303eeA07b8
- Resolution
- 3
- Source
- Human rhinovirus 14
- Molecule
- Human rhinovirus 14 coat protein (subunit VP1); Human rhinovirus 14 coat protein (subunit…
- UniProt
- P03303
- Pockets
- 12 · best druggability 0.79
Structure
x-ray diffraction · resolution 3 · 4 distinct chains · 12% helix, 32% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| 1 | Human rhinovirus 14 coat protein (subunit VP1) | protein | 273 | 11% helix, 32% strand | P03303 |
| 2 | Human rhinovirus 14 coat protein (subunit VP2) | protein | 255 | 15% helix, 37% strand | P03303 |
| 3 | Human rhinovirus 14 coat protein (subunit VP3) | protein | 236 | 9% helix, 32% strand | P03303 |
| 4 | Human rhinovirus 14 coat protein (subunit VP4) | protein | 40 | 18% helix, 3% strand | P03303 |
Pockets
12 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 205 | 0.79 | 0.93 | 39 | empty |
| 2 | 169 | 0.45 | 0.75 | 35 | empty |
| 3 | 122 | 0.41 | 0.76 | 21 | empty |
| 4 | 119 | 0.41 | 0.75 | 25 | empty |
| 5 | 86 | 0.38 | 0.77 | 18 | empty |
Interfaces
6 interfaces between chains.
- 1–3 · 4127 Ų buried · 70 hydrogen bonds · protein-protein
- 1–2 · 2125 Ų buried · 45 hydrogen bonds · protein-protein
- 2–3 · 1703 Ų buried · 15 hydrogen bonds · protein-protein
- 1–4 · 953 Ų buried · 14 hydrogen bonds · protein-protein
- 3–4 · 903 Ų buried · 14 hydrogen bonds · protein-protein
Compared structures
- 2RMU · Three-dimensional structures of drug-resistant mutants of human rhinovirus 14 · the same entry in another collection · chain 1 against 1, 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 P03303
- Elsewhere: RCSB PDB 2RMU · PDBe 2RMU · UniProt P03303
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