Research workbench
X-ray crystallographic structure of crimean-congo haemorrhagic fever virus nucleoprotein
Analyse X-ray crystallographic structure of crimean-congo haemorrhagic fever virus… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 4AQF
- Type
- protein
- Length
- 1,406 residues
- Chains
- 3
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Nucleoprotein
- UniProt
- P89522
- Ligands
- SO4
- Pockets
- 11 · best druggability 0.85
Structure
x-ray diffraction · 3 distinct chains · 63% helix, 2% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Nucleoprotein | protein | 466 | 63% helix, 2% strand | P89522 |
| B | Nucleoprotein | protein | 474 | 62% helix, 2% strand | P89522 |
| C | Nucleoprotein | protein | 466 | 64% helix, 3% strand | P89522 |
Ligands and binding sites
- SO4 · Sulfate ion · ion · 4 copies · chains A, C, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
11 pockets found on a 1 Å grid, 5 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 995 | 0.85 | 0.85 | 86 | empty |
| 2 | 1193 | 0.83 | 0.84 | 99 | empty |
| 3 | 1177 | 0.81 | 0.82 | 82 | empty |
| 4 | 224 | 0.64 | 0.83 | 40 | empty |
| 5 | 146 | 0.63 | 0.85 | 31 | empty |
Interfaces
2 interfaces between chains.
- A–B · 1160 Ų buried · 16 hydrogen bonds · protein-protein
- A–C · 969 Ų buried · 5 hydrogen bonds · protein-protein
Compared structures
- 4AQF · X-ray crystallographic structure of Crimean-congo haemorrhagic fever virus nucleoprotein · 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 P89522
- Elsewhere: RCSB PDB 4AQF · PDBe 4AQF · UniProt P89522
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