7CVZ
Cryo-EM structure of Chikungunya virus in complex with Fab fragments of mAb CHK-263
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0004252 | molecular_function | serine-type endopeptidase activity |
| A | 0019028 | cellular_component | viral capsid |
| A | 0055036 | cellular_component | virion membrane |
| B | 0005198 | molecular_function | structural molecule activity |
| B | 0019028 | cellular_component | viral capsid |
| C | 0004252 | molecular_function | serine-type endopeptidase activity |
| C | 0006508 | biological_process | proteolysis |
| D | 0004252 | molecular_function | serine-type endopeptidase activity |
| D | 0019028 | cellular_component | viral capsid |
| D | 0055036 | cellular_component | virion membrane |
| E | 0005198 | molecular_function | structural molecule activity |
| E | 0019028 | cellular_component | viral capsid |
| F | 0004252 | molecular_function | serine-type endopeptidase activity |
| F | 0006508 | biological_process | proteolysis |
| G | 0004252 | molecular_function | serine-type endopeptidase activity |
| G | 0019028 | cellular_component | viral capsid |
| G | 0055036 | cellular_component | virion membrane |
| H | 0005198 | molecular_function | structural molecule activity |
| H | 0019028 | cellular_component | viral capsid |
| I | 0004252 | molecular_function | serine-type endopeptidase activity |
| I | 0006508 | biological_process | proteolysis |
| J | 0004252 | molecular_function | serine-type endopeptidase activity |
| J | 0019028 | cellular_component | viral capsid |
| J | 0055036 | cellular_component | virion membrane |
| K | 0005198 | molecular_function | structural molecule activity |
| K | 0019028 | cellular_component | viral capsid |
| L | 0004252 | molecular_function | serine-type endopeptidase activity |
| L | 0006508 | biological_process | proteolysis |
Functional Information from PROSITE/UniProt
| site_id | PS00290 |
| Number of Residues | 7 |
| Details | IG_MHC Immunoglobulins and major histocompatibility complex proteins signature. YTCEATH |
| Chain | Residue | Details |
| P | TYR192-HIS198 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 12 |
| Details | ACT_SITE: Charge relay system => ECO:0000255|PROSITE-ProRule:PRU01027 |
| Chain | Residue | Details |
| F | HIS139 | |
| F | ASP161 | |
| F | SER213 | |
| L | HIS139 | |
| L | ASP161 | |
| L | SER213 | |
| I | HIS139 | |
| I | ASP161 | |
| I | SER213 | |
| C | HIS139 | |
| C | ASP161 | |
| C | SER213 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 8 |
| Details | SITE: Involved in dimerization of the capsid protein => ECO:0000250|UniProtKB:Q86925 |
| Chain | Residue | Details |
| F | TYR187 | |
| F | ASN220 | |
| L | TYR187 | |
| L | ASN220 | |
| I | TYR187 | |
| I | ASN220 | |
| C | TYR187 | |
| C | ASN220 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 4 |
| Details | SITE: Cleavage; by autolysis => ECO:0000250|UniProtKB:P03315 |
| Chain | Residue | Details |
| F | TRP261 | |
| L | TRP261 | |
| I | TRP261 | |
| C | TRP261 |
| site_id | SWS_FT_FI4 |
| Number of Residues | 12 |
| Details | LIPID: S-palmitoyl cysteine; by host => ECO:0000250 |
| Chain | Residue | Details |
| E | CYS396 | |
| E | CYS416 | |
| E | CYS417 | |
| H | CYS396 | |
| H | CYS416 | |
| H | CYS417 | |
| K | CYS396 | |
| K | CYS416 | |
| K | CYS417 | |
| B | CYS396 | |
| B | CYS416 | |
| B | CYS417 |
| site_id | SWS_FT_FI5 |
| Number of Residues | 8 |
| Details | CARBOHYD: N-linked (GlcNAc...) asparagine; by host => ECO:0000255 |
| Chain | Residue | Details |
| E | ASN263 | |
| E | ASN345 | |
| H | ASN263 | |
| H | ASN345 | |
| K | ASN263 | |
| K | ASN345 | |
| B | ASN263 | |
| B | ASN345 |
