5I2M
CRYSTAL STRUCTURE OF VSV-INDIANA (MUDD-SUMMERS STRAIN) GLYCOPROTEIN UNDER ITS ACIDIC CONFORMATION
Replaces: 2CMZFunctional Information from GO Data
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 | 267 |
| Details | Region: {"description":"Trimerization","evidences":[{"source":"PubMed","id":"17289996","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 357 |
| Details | Region: {"description":"Fusion peptide","evidences":[{"source":"PubMed","id":"17289996","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 6 |
| Details | Site: {"description":"Involved in the interaction with host LDL receptor"} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 9 |
| Details | Site: {"description":"pH sensor in the pre-fusion state","evidences":[{"source":"PubMed","id":"17289996","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI5 |
| Number of Residues | 3 |
| Details | Modified residue: {"description":"N6-methyllysine; by host","evidences":[{"source":"PDB","id":"5OY9","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI6 |
| Number of Residues | 3 |
| Details | Glycosylation: {"description":"N-linked (GlcNAc...) asparagine; by host","evidences":[{"source":"PubMed","id":"17289996","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"5I2S","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI7 |
| Number of Residues | 3 |
| Details | Glycosylation: {"description":"N-linked (GlcNAc...) asparagine; by host","evidences":[{"source":"PubMed","id":"17289996","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"29531262","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"5I2S","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"5OY9","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
