Research workbench
Human rhinovirus serotype 2 (HRV2)
Analyse Human rhinovirus serotype 2 (HRV2) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1FPN
- Type
- protein
- Length
- 781 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
- P04936
- Ligands
- DAO
- Pockets
- 13 · best druggability 0.80
Structure
x-ray diffraction · 4 distinct chains · 10% helix, 33% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| 1 | Coat protein VP1 | protein | 269 | 10% helix, 31% strand | P04936 |
| 2 | Coat protein VP2 | protein | 250 | 12% helix, 37% strand | P04936 |
| 3 | Coat protein VP3 | protein | 237 | 9% helix, 32% strand | P04936 |
| 4 | Coat protein VP4 | protein | 25 | 12% helix, 16% strand | P04936 |
Ligands and binding sites
- DAO · Lauric acid · ligand · chains 1
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
13 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 208 | 0.80 | 0.93 | 39 | DAO |
| 2 | 237 | 0.57 | 0.78 | 25 | empty |
| 3 | 215 | 0.50 | 0.75 | 43 | empty |
| 4 | 128 | 0.49 | 0.79 | 23 | empty |
| 5 | 79 | 0.45 | 0.81 | 16 | empty |
Interfaces
5 interfaces between chains.
- 1–3 · 4135 Ų buried · 66 hydrogen bonds · protein-protein
- 1–2 · 2040 Ų buried · 40 hydrogen bonds · protein-protein
- 2–3 · 1690 Ų buried · 24 hydrogen bonds · protein-protein
- 3–4 · 393 Ų buried · 7 hydrogen bonds · protein-protein
- 1–4 · 360 Ų buried · 7 hydrogen bonds · protein-protein
Compared structures
- 1FPN · Human rhinovirus serotype 2 (HRV2) · 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 P04936
- Elsewhere: RCSB PDB 1FPN · PDBe 1FPN · UniProt P04936
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