Research workbench
Structure of the nucleoprotein from rift valley fever virus
Analyse Structure of the nucleoprotein from rift valley fever virus in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3OV9
- Type
- protein
- Length
- 733 residues
- Chains
- 3
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Nucleoprotein
- UniProt
- P21700
- Ligands
- NA, NO2
- Pockets
- 4 · best druggability 0.79
Structure
x-ray diffraction · 2 distinct chains · 69% helix, 1% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Nucleoprotein | protein | 245 | 69% helix, 1% strand | P21700 |
| B, C | Nucleoprotein | protein | 244 | 69% helix, 1% strand | P21700 |
Ligands and binding sites
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
4 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 1093 | 0.79 | 0.81 | 124 | NO2, NA |
| 2 | 844 | 0.73 | 0.78 | 84 | NO2 |
| 3 | 113 | 0.44 | 0.78 | 20 | empty |
| 4 | 50 | 0.30 | 0.77 | 11 | empty |
Interfaces
2 interfaces between chains.
- A–B · 1725 Ų buried · 22 hydrogen bonds · protein-protein
- B–C · 442 Ų buried · 8 hydrogen bonds · protein-protein
Compared structures
- 3OV9 · Structure of the Nucleoprotein from Rift Valley Fever Virus · 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 P21700
- Elsewhere: RCSB PDB 3OV9 · PDBe 3OV9 · UniProt P21700
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