3OV9
Structure of the Nucleoprotein from Rift Valley Fever Virus
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0003723 | molecular_function | RNA binding |
| A | 0019013 | cellular_component | viral nucleocapsid |
| A | 0019028 | cellular_component | viral capsid |
| A | 0019029 | cellular_component | helical viral capsid |
| A | 0030430 | cellular_component | host cell cytoplasm |
| A | 0042025 | cellular_component | host cell nucleus |
| A | 0044172 | cellular_component | host cell endoplasmic reticulum-Golgi intermediate compartment |
| A | 0044177 | cellular_component | host cell Golgi apparatus |
| A | 0044423 | cellular_component | virion component |
| A | 1990904 | cellular_component | ribonucleoprotein complex |
| B | 0003723 | molecular_function | RNA binding |
| B | 0019013 | cellular_component | viral nucleocapsid |
| B | 0019028 | cellular_component | viral capsid |
| B | 0019029 | cellular_component | helical viral capsid |
| B | 0030430 | cellular_component | host cell cytoplasm |
| B | 0042025 | cellular_component | host cell nucleus |
| B | 0044172 | cellular_component | host cell endoplasmic reticulum-Golgi intermediate compartment |
| B | 0044177 | cellular_component | host cell Golgi apparatus |
| B | 0044423 | cellular_component | virion component |
| B | 1990904 | cellular_component | ribonucleoprotein complex |
| C | 0003723 | molecular_function | RNA binding |
| C | 0019013 | cellular_component | viral nucleocapsid |
| C | 0019028 | cellular_component | viral capsid |
| C | 0019029 | cellular_component | helical viral capsid |
| C | 0030430 | cellular_component | host cell cytoplasm |
| C | 0042025 | cellular_component | host cell nucleus |
| C | 0044172 | cellular_component | host cell endoplasmic reticulum-Golgi intermediate compartment |
| C | 0044177 | cellular_component | host cell Golgi apparatus |
| C | 0044423 | cellular_component | virion component |
| C | 1990904 | cellular_component | ribonucleoprotein complex |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 9 |
| Details | BINDING SITE FOR RESIDUE NO2 A 246 |
| Chain | Residue |
| A | GLY32 |
| A | PHE33 |
| A | ALA202 |
| A | ALA203 |
| A | SER206 |
| A | HOH258 |
| A | HOH259 |
| A | HOH328 |
| A | HOH336 |
| site_id | AC2 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE NA A 247 |
| Chain | Residue |
| A | SER206 |
| A | ILE209 |
| A | HOH564 |
| site_id | AC3 |
| Number of Residues | 10 |
| Details | BINDING SITE FOR RESIDUE NO2 B 246 |
| Chain | Residue |
| B | GLN31 |
| B | GLY32 |
| B | PHE33 |
| B | ALA202 |
| B | ALA203 |
| B | SER206 |
| B | HOH258 |
| B | HOH262 |
| B | HOH278 |
| B | HOH358 |
| site_id | AC4 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE NA B 247 |
| Chain | Residue |
| A | HOH960 |
| B | ALA109 |
| B | SER148 |
| B | GLY151 |
| B | HOH356 |
| site_id | AC5 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE NO2 C 246 |
| Chain | Residue |
| C | GLY32 |
| C | PHE33 |
| C | ALA202 |
| C | ALA203 |
| C | SER206 |
| C | HOH262 |
| C | HOH284 |
| C | HOH400 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 21 |
| Details | SITE: RNA-binding => ECO:0000250|UniProtKB:D3K5I7 |
| Chain | Residue | Details |
| A | TYR30 | |
| A | PHE33 | |
| A | ASN66 | |
| A | LYS67 | |
| A | ARG70 | |
| A | ARG99 | |
| A | ARG106 | |
| B | TYR30 | |
| B | PHE33 | |
| B | ASN66 | |
| B | LYS67 | |
| B | ARG70 | |
| B | ARG99 | |
| B | ARG106 | |
| C | TYR30 | |
| C | PHE33 | |
| C | ASN66 | |
| C | LYS67 | |
| C | ARG70 | |
| C | ARG99 | |
| C | ARG106 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 3 |
| Details | SITE: Important for dimerization => ECO:0000250|UniProtKB:D3K5I7 |
| Chain | Residue | Details |
| A | TRP125 | |
| B | TRP125 | |
| C | TRP125 |
