4XZE
The crystal structure of Hazara virus nucleoprotein
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0003723 | molecular_function | RNA binding |
| A | 0016787 | molecular_function | hydrolase activity |
| A | 0019013 | cellular_component | viral nucleocapsid |
| A | 0019029 | cellular_component | helical viral capsid |
| A | 1990904 | cellular_component | ribonucleoprotein complex |
| B | 0003723 | molecular_function | RNA binding |
| B | 0016787 | molecular_function | hydrolase activity |
| B | 0019013 | cellular_component | viral nucleocapsid |
| B | 0019029 | cellular_component | helical viral capsid |
| B | 1990904 | cellular_component | ribonucleoprotein complex |
| C | 0003723 | molecular_function | RNA binding |
| C | 0016787 | molecular_function | hydrolase activity |
| C | 0019013 | cellular_component | viral nucleocapsid |
| C | 0019029 | cellular_component | helical viral capsid |
| C | 1990904 | cellular_component | ribonucleoprotein complex |
| D | 0003723 | molecular_function | RNA binding |
| D | 0016787 | molecular_function | hydrolase activity |
| D | 0019013 | cellular_component | viral nucleocapsid |
| D | 0019029 | cellular_component | helical viral capsid |
| D | 1990904 | cellular_component | ribonucleoprotein complex |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 28 |
| Details | SITE: Homooligomerization => ECO:0000269|PubMed:26715309 |
| Chain | Residue | Details |
| A | PHE216 | |
| B | GLN270 | |
| B | VAL271 | |
| B | LYS275 | |
| B | LEU279 | |
| B | PRO355 | |
| C | PHE216 | |
| C | TRP263 | |
| C | GLN270 | |
| C | VAL271 | |
| C | LYS275 | |
| A | TRP263 | |
| C | LEU279 | |
| C | PRO355 | |
| D | PHE216 | |
| D | TRP263 | |
| D | GLN270 | |
| D | VAL271 | |
| D | LYS275 | |
| D | LEU279 | |
| D | PRO355 | |
| A | GLN270 | |
| A | VAL271 | |
| A | LYS275 | |
| A | LEU279 | |
| A | PRO355 | |
| B | PHE216 | |
| B | TRP263 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 4 |
| Details | SITE: Cleavage by host CASP3/caspase 3 => ECO:0000269|PubMed:30720418, ECO:0000269|PubMed:31118258 |
| Chain | Residue | Details |
| A | ASP272 | |
| B | ASP272 | |
| C | ASP272 | |
| D | ASP272 |
