6XOB
CryoEM structure of Eastern Equine Encephalitis (EEEV) VLP with Fab EEEV-143.
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. YACEVTH |
Chain | Residue | Details |
N | TYR191-HIS197 |
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 |
C | HIS138 | |
L | HIS138 | |
L | ASP160 | |
L | SER212 | |
C | ASP160 | |
C | SER212 | |
F | HIS138 | |
F | ASP160 | |
F | SER212 | |
I | HIS138 | |
I | ASP160 | |
I | SER212 |
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 |
C | TYR186 | |
C | ASN219 | |
F | TYR186 | |
F | ASN219 | |
I | TYR186 | |
I | ASN219 | |
L | TYR186 | |
L | ASN219 |
site_id | SWS_FT_FI3 |
Number of Residues | 4 |
Details | SITE: Cleavage; by autolysis => ECO:0000250|UniProtKB:P03315 |
Chain | Residue | Details |
C | TRP261 | |
F | TRP261 | |
I | TRP261 | |
L | TRP261 |
site_id | SWS_FT_FI4 |
Number of Residues | 4 |
Details | MOD_RES: Phosphoserine => ECO:0000250|UniProtKB:P09592 |
Chain | Residue | Details |
C | SER110 | |
F | SER110 | |
I | SER110 | |
L | SER110 |
site_id | SWS_FT_FI5 |
Number of Residues | 4 |
Details | MOD_RES: Phosphothreonine => ECO:0000250|UniProtKB:P09592 |
Chain | Residue | Details |
C | THR113 | |
K | CYS393 | |
K | CYS413 | |
K | CYS414 | |
F | THR113 | |
I | THR113 | |
L | THR113 | |
E | CYS413 | |
E | CYS414 | |
H | CYS393 | |
H | CYS413 | |
H | CYS414 |