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 | 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 | 1990904 | cellular_component | ribonucleoprotein complex |
B | 0003723 | molecular_function | RNA binding |
B | 0019013 | cellular_component | viral nucleocapsid |
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 | 1990904 | cellular_component | ribonucleoprotein complex |
C | 0003723 | molecular_function | RNA binding |
C | 0019013 | cellular_component | viral nucleocapsid |
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 | 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 | |
B | ASN66 | |
B | LYS67 | |
B | ARG70 | |
B | ARG99 | |
B | ARG106 | |
C | TYR30 | |
C | PHE33 | |
C | ASN66 | |
C | LYS67 | |
C | ARG70 | |
A | PHE33 | |
C | ARG99 | |
C | ARG106 | |
A | ASN66 | |
A | LYS67 | |
A | ARG70 | |
A | ARG99 | |
A | ARG106 | |
B | TYR30 | |
B | PHE33 |
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 |