5I2M
CRYSTAL STRUCTURE OF VSV-INDIANA (MUDD-SUMMERS STRAIN) GLYCOPROTEIN UNDER ITS ACIDIC CONFORMATION
Replaces: 2CMZFunctional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0016020 | cellular_component | membrane |
| A | 0019031 | cellular_component | viral envelope |
| A | 0019062 | biological_process | virion attachment to host cell |
| A | 0039654 | biological_process | fusion of virus membrane with host endosome membrane |
| A | 0046718 | biological_process | symbiont entry into host cell |
| A | 0055036 | cellular_component | virion membrane |
| A | 0075512 | biological_process | clathrin-dependent endocytosis of virus by host cell |
| B | 0016020 | cellular_component | membrane |
| B | 0019031 | cellular_component | viral envelope |
| B | 0019062 | biological_process | virion attachment to host cell |
| B | 0039654 | biological_process | fusion of virus membrane with host endosome membrane |
| B | 0046718 | biological_process | symbiont entry into host cell |
| B | 0055036 | cellular_component | virion membrane |
| B | 0075512 | biological_process | clathrin-dependent endocytosis of virus by host cell |
| C | 0016020 | cellular_component | membrane |
| C | 0019031 | cellular_component | viral envelope |
| C | 0019062 | biological_process | virion attachment to host cell |
| C | 0039654 | biological_process | fusion of virus membrane with host endosome membrane |
| C | 0046718 | biological_process | symbiont entry into host cell |
| C | 0055036 | cellular_component | virion membrane |
| C | 0075512 | biological_process | clathrin-dependent endocytosis of virus by host cell |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 7 |
| Details | binding site for residue PE4 A 501 |
| Chain | Residue |
| A | LYS220 |
| A | TRP227 |
| A | PHE245 |
| A | ALA246 |
| A | ARG249 |
| A | PHE250 |
| A | GLU252 |
| site_id | AC2 |
| Number of Residues | 10 |
| Details | binding site for residue PE4 B 501 |
| Chain | Residue |
| B | LYS220 |
| B | TRP227 |
| B | ALA246 |
| B | ARG249 |
| B | PHE250 |
| B | GLU252 |
| B | HOH658 |
| B | HOH749 |
| A | GLU327 |
| A | HOH673 |
| site_id | AC3 |
| Number of Residues | 10 |
| Details | binding site for residue PE4 B 502 |
| Chain | Residue |
| B | ILE339 |
| B | LEU340 |
| B | SER341 |
| B | ARG342 |
| B | VAL344 |
| B | ARG375 |
| B | THR376 |
| B | SER377 |
| B | SER378 |
| B | GLY379 |
| site_id | AC4 |
| Number of Residues | 6 |
| Details | binding site for residue PE4 B 503 |
| Chain | Residue |
| B | PRO338 |
| B | ILE339 |
| B | SER378 |
| B | LYS381 |
| B | PHE382 |
| C | HIS33 |
| site_id | AC5 |
| Number of Residues | 9 |
| Details | binding site for residue PE4 C 501 |
| Chain | Residue |
| C | ASN20 |
| C | LYS220 |
| C | TRP227 |
| C | PHE245 |
| C | ALA246 |
| C | ARG249 |
| C | PHE250 |
| C | GLU252 |
| C | HOH645 |
| site_id | AC6 |
| Number of Residues | 5 |
| Details | binding site for residue CA C 502 |
| Chain | Residue |
| C | GLU191 |
| C | ASP192 |
| C | ASP192 |
| C | GLU194 |
| C | HOH670 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 6 |
| Details | CARBOHYD: N-linked (GlcNAc...) asparagine; by host => ECO:0000255 |
| Chain | Residue | Details |
| A | ASN163 | |
| A | ASN320 | |
| B | ASN163 | |
| B | ASN320 | |
| C | ASN163 | |
| C | ASN320 |
