7V4T
Cryo-EM structure of Alphavirus M1
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 |
| E | 0004252 | molecular_function | serine-type endopeptidase activity |
| E | 0019028 | cellular_component | viral capsid |
| E | 0055036 | cellular_component | virion membrane |
| F | 0005198 | molecular_function | structural molecule activity |
| F | 0019028 | cellular_component | viral capsid |
| G | 0004252 | molecular_function | serine-type endopeptidase activity |
| G | 0006508 | biological_process | proteolysis |
| I | 0004252 | molecular_function | serine-type endopeptidase activity |
| I | 0019028 | cellular_component | viral capsid |
| I | 0055036 | cellular_component | virion membrane |
| J | 0005198 | molecular_function | structural molecule activity |
| J | 0019028 | cellular_component | viral capsid |
| K | 0004252 | molecular_function | serine-type endopeptidase activity |
| K | 0006508 | biological_process | proteolysis |
| M | 0004252 | molecular_function | serine-type endopeptidase activity |
| M | 0019028 | cellular_component | viral capsid |
| M | 0055036 | cellular_component | virion membrane |
| N | 0005198 | molecular_function | structural molecule activity |
| N | 0019028 | cellular_component | viral capsid |
| O | 0004252 | molecular_function | serine-type endopeptidase activity |
| O | 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 |
| C | VAL146 | |
| O | VAL146 | |
| O | LEU168 | |
| O | GLY220 | |
| C | LEU168 | |
| C | GLY220 | |
| G | VAL146 | |
| G | LEU168 | |
| G | GLY220 | |
| K | VAL146 | |
| K | LEU168 | |
| K | GLY220 |
| 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 | ASN194 | |
| C | LYS227 | |
| G | ASN194 | |
| G | LYS227 | |
| K | ASN194 | |
| K | LYS227 | |
| O | ASN194 | |
| O | LYS227 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 4 |
| Details | SITE: Cleavage; by autolysis => ECO:0000250|UniProtKB:P03315 |
| Chain | Residue | Details |
| B | SER384-ALA422 | |
| F | SER384-ALA422 | |
| J | SER384-ALA422 | |
| N | SER384-ALA422 |
| site_id | SWS_FT_FI4 |
| Number of Residues | 4 |
| Details | SITE: Cleavage; by host signal peptidase => ECO:0000250 |
| Chain | Residue | Details |
| B | ALA422 | |
| F | ALA422 | |
| J | ALA422 | |
| N | ALA422 |
| site_id | SWS_FT_FI5 |
| Number of Residues | 12 |
| Details | LIPID: S-palmitoyl cysteine; by host => ECO:0000250 |
| Chain | Residue | Details |
| B | CYS395 | |
| N | CYS395 | |
| N | CYS415 | |
| N | CYS416 | |
| B | CYS415 | |
| B | CYS416 | |
| F | CYS395 | |
| F | CYS415 | |
| F | CYS416 | |
| J | CYS395 | |
| J | CYS415 | |
| J | CYS416 |
| site_id | SWS_FT_FI6 |
| Number of Residues | 8 |
| Details | CARBOHYD: N-linked (GlcNAc...) asparagine; by host => ECO:0000255 |
| Chain | Residue | Details |
| B | ASN200 | |
| B | ASN262 | |
| F | ASN200 | |
| F | ASN262 | |
| J | ASN200 | |
| J | ASN262 | |
| N | ASN200 | |
| N | ASN262 |
