4JRA
CRYSTAL STRUCTURE OF THE BOTULINUM NEUROTOXIN A RECEPTOR-BINDING DOMAIN IN COMPLEX WITH THE LUMINAL DOMAIN Of SV2C
Functional Information from GO Data
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 1 |
Details | BINDING SITE FOR RESIDUE CL A 1301 |
Chain | Residue |
A | PHE1100 |
site_id | AC2 |
Number of Residues | 1 |
Details | BINDING SITE FOR RESIDUE CL A 1302 |
Chain | Residue |
A | ARG1034 |
site_id | AC3 |
Number of Residues | 1 |
Details | BINDING SITE FOR RESIDUE CL A 1303 |
Chain | Residue |
A | GLU1210 |
site_id | AC4 |
Number of Residues | 2 |
Details | BINDING SITE FOR RESIDUE CL A 1304 |
Chain | Residue |
A | LEU1097 |
A | LYS1098 |
site_id | AC5 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE CL A 1305 |
Chain | Residue |
A | SER1002 |
A | TYR1010 |
A | NA1306 |
site_id | AC6 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE NA A 1306 |
Chain | Residue |
A | SER1008 |
A | CL1305 |
A | SER1002 |
site_id | AC7 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE NA A 1307 |
Chain | Residue |
A | ASP1099 |
A | TYR1104 |
A | TYR1111 |
site_id | AC8 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE CL A 1308 |
Chain | Residue |
A | TYR980 |
A | GLN1003 |
A | MET1004 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 6 |
Details | Motif: {"description":"Host ganglioside-binding motif","evidences":[{"source":"UniProtKB","id":"P0DPI0","evidenceCode":"ECO:0000250"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI2 |
Number of Residues | 88 |
Details | Region: {"description":"(Microbial infection) C.botulinum neurotoxin type A-binding","evidences":[{"source":"PubMed","id":"27294781","evidenceCode":"ECO:0000269"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI3 |
Number of Residues | 3 |
Details | Glycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"evidenceCode":"ECO:0000255"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI4 |
Number of Residues | 2 |
Details | Glycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"source":"PubMed","id":"27313224","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"5JLV","evidenceCode":"ECO:0007744"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI5 |
Number of Residues | 2 |
Details | Glycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"source":"PubMed","id":"27313224","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"28252640","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"5JLV","evidenceCode":"ECO:0007744"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI6 |
Number of Residues | 1 |
Details | Glycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"27313224","evidenceCode":"ECO:0000269"}]} |
Chain | Residue | Details |