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 | |
C | HIS139 | |
C | ASP161 | |
C | SER213 | |
F | ASP161 | |
F | SER213 | |
L | HIS139 | |
L | ASP161 | |
L | SER213 | |
I | HIS139 | |
I | ASP161 | |
I | 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 | |
B | CYS396 | |
B | CYS416 | |
B | CYS417 | |
E | CYS416 | |
E | CYS417 | |
H | CYS396 | |
H | CYS416 | |
H | CYS417 | |
K | CYS396 | |
K | CYS416 | |
K | 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 |