7CVY
Cryo-EM structure of Chikungunya virus in complex with Fab fragments of mAb CHK-124
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 |
F | 0004252 | molecular_function | serine-type endopeptidase activity |
F | 0019028 | cellular_component | viral capsid |
F | 0055036 | cellular_component | virion membrane |
G | 0005198 | molecular_function | structural molecule activity |
G | 0019028 | cellular_component | viral capsid |
H | 0004252 | molecular_function | serine-type endopeptidase activity |
H | 0006508 | biological_process | proteolysis |
K | 0004252 | molecular_function | serine-type endopeptidase activity |
K | 0019028 | cellular_component | viral capsid |
K | 0055036 | cellular_component | virion membrane |
L | 0005198 | molecular_function | structural molecule activity |
L | 0019028 | cellular_component | viral capsid |
M | 0004252 | molecular_function | serine-type endopeptidase activity |
M | 0006508 | biological_process | proteolysis |
P | 0004252 | molecular_function | serine-type endopeptidase activity |
P | 0019028 | cellular_component | viral capsid |
P | 0055036 | cellular_component | virion membrane |
Q | 0005198 | molecular_function | structural molecule activity |
Q | 0019028 | cellular_component | viral capsid |
R | 0004252 | molecular_function | serine-type endopeptidase activity |
R | 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 |
E | 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 |
H | HIS139 | |
M | HIS139 | |
M | ASP161 | |
M | SER213 | |
H | ASP161 | |
H | SER213 | |
C | HIS139 | |
C | ASP161 | |
C | SER213 | |
R | HIS139 | |
R | ASP161 | |
R | 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 |
H | TYR187 | |
H | ASN220 | |
C | TYR187 | |
C | ASN220 | |
R | TYR187 | |
R | ASN220 | |
M | TYR187 | |
M | ASN220 |
site_id | SWS_FT_FI3 |
Number of Residues | 4 |
Details | SITE: Cleavage; by autolysis => ECO:0000250|UniProtKB:P03315 |
Chain | Residue | Details |
H | TRP261 | |
C | TRP261 | |
R | TRP261 | |
M | TRP261 |
site_id | SWS_FT_FI4 |
Number of Residues | 12 |
Details | LIPID: S-palmitoyl cysteine; by host => ECO:0000250 |
Chain | Residue | Details |
G | CYS396 | |
L | CYS396 | |
L | CYS416 | |
L | CYS417 | |
G | CYS416 | |
G | CYS417 | |
B | CYS396 | |
B | CYS416 | |
B | CYS417 | |
Q | CYS396 | |
Q | CYS416 | |
Q | CYS417 |
site_id | SWS_FT_FI5 |
Number of Residues | 8 |
Details | CARBOHYD: N-linked (GlcNAc...) asparagine; by host => ECO:0000255 |
Chain | Residue | Details |
G | ASN263 | |
G | ASN345 | |
B | ASN263 | |
B | ASN345 | |
Q | ASN263 | |
Q | ASN345 | |
L | ASN263 | |
L | ASN345 |