8DWX
Chikungunya VLP in complex with neutralizing Fab 506.C01 (asymmetric unit)
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 | 0004252 | molecular_function | serine-type endopeptidase activity |
| B | 0019028 | cellular_component | viral capsid |
| B | 0055036 | cellular_component | virion membrane |
| C | 0004252 | molecular_function | serine-type endopeptidase activity |
| C | 0019028 | cellular_component | viral capsid |
| C | 0055036 | cellular_component | virion membrane |
| D | 0004252 | molecular_function | serine-type endopeptidase activity |
| D | 0019028 | cellular_component | viral capsid |
| D | 0055036 | cellular_component | virion membrane |
| M | 0005198 | molecular_function | structural molecule activity |
| M | 0019028 | cellular_component | viral capsid |
| N | 0005198 | molecular_function | structural molecule activity |
| N | 0019028 | cellular_component | viral capsid |
| O | 0005198 | molecular_function | structural molecule activity |
| O | 0019028 | cellular_component | viral capsid |
| P | 0005198 | molecular_function | structural molecule activity |
| P | 0019028 | cellular_component | viral capsid |
| Q | 0004252 | molecular_function | serine-type endopeptidase activity |
| Q | 0006508 | biological_process | proteolysis |
| R | 0004252 | molecular_function | serine-type endopeptidase activity |
| R | 0006508 | biological_process | proteolysis |
| S | 0004252 | molecular_function | serine-type endopeptidase activity |
| S | 0006508 | biological_process | proteolysis |
| T | 0004252 | molecular_function | serine-type endopeptidase activity |
| T | 0006508 | biological_process | proteolysis |
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 |
| Q | HIS139 | |
| T | HIS139 | |
| T | ASP161 | |
| T | SER213 | |
| Q | ASP161 | |
| Q | SER213 | |
| R | HIS139 | |
| R | ASP161 | |
| R | SER213 | |
| S | HIS139 | |
| S | ASP161 | |
| S | 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 |
| Q | TYR187 | |
| Q | ASN220 | |
| R | TYR187 | |
| R | ASN220 | |
| S | TYR187 | |
| S | ASN220 | |
| T | TYR187 | |
| T | ASN220 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 4 |
| Details | SITE: Cleavage; by autolysis => ECO:0000250|UniProtKB:P03315 |
| Chain | Residue | Details |
| Q | TRP261 | |
| R | TRP261 | |
| S | TRP261 | |
| T | TRP261 |
| site_id | SWS_FT_FI4 |
| Number of Residues | 12 |
| Details | LIPID: S-palmitoyl cysteine; by host => ECO:0000250 |
| Chain | Residue | Details |
| M | CYS396 | |
| P | CYS396 | |
| P | CYS416 | |
| P | CYS417 | |
| M | CYS416 | |
| M | CYS417 | |
| N | CYS396 | |
| N | CYS416 | |
| N | CYS417 | |
| O | CYS396 | |
| O | CYS416 | |
| O | CYS417 |
| site_id | SWS_FT_FI5 |
| Number of Residues | 8 |
| Details | CARBOHYD: N-linked (GlcNAc...) asparagine; by host => ECO:0000255 |
| Chain | Residue | Details |
| M | ASN263 | |
| M | ASN345 | |
| N | ASN263 | |
| N | ASN345 | |
| O | ASN263 | |
| O | ASN345 | |
| P | ASN263 | |
| P | ASN345 |
