3FFZ
Domain organization in Clostridium butulinum neurotoxin type E is unique: Its implication in faster translocation
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0004222 | molecular_function | metalloendopeptidase activity |
A | 0005576 | cellular_component | extracellular region |
A | 0006508 | biological_process | proteolysis |
A | 0008233 | molecular_function | peptidase activity |
A | 0008237 | molecular_function | metallopeptidase activity |
A | 0008270 | molecular_function | zinc ion binding |
A | 0008289 | molecular_function | lipid binding |
A | 0008320 | molecular_function | protein transmembrane transporter activity |
A | 0016020 | cellular_component | membrane |
A | 0016787 | molecular_function | hydrolase activity |
A | 0020002 | cellular_component | host cell plasma membrane |
A | 0030430 | cellular_component | host cell cytoplasm |
A | 0033644 | cellular_component | host cell membrane |
A | 0035821 | biological_process | modulation of process of another organism |
A | 0044161 | cellular_component | host cell cytoplasmic vesicle |
A | 0044164 | cellular_component | host cell cytosol |
A | 0044221 | cellular_component | host cell synapse |
A | 0044231 | cellular_component | host cell presynaptic membrane |
A | 0046872 | molecular_function | metal ion binding |
A | 0071806 | biological_process | protein transmembrane transport |
A | 0090729 | molecular_function | toxin activity |
B | 0004222 | molecular_function | metalloendopeptidase activity |
B | 0005576 | cellular_component | extracellular region |
B | 0006508 | biological_process | proteolysis |
B | 0008233 | molecular_function | peptidase activity |
B | 0008237 | molecular_function | metallopeptidase activity |
B | 0008270 | molecular_function | zinc ion binding |
B | 0008289 | molecular_function | lipid binding |
B | 0008320 | molecular_function | protein transmembrane transporter activity |
B | 0016020 | cellular_component | membrane |
B | 0016787 | molecular_function | hydrolase activity |
B | 0020002 | cellular_component | host cell plasma membrane |
B | 0030430 | cellular_component | host cell cytoplasm |
B | 0033644 | cellular_component | host cell membrane |
B | 0035821 | biological_process | modulation of process of another organism |
B | 0044161 | cellular_component | host cell cytoplasmic vesicle |
B | 0044164 | cellular_component | host cell cytosol |
B | 0044221 | cellular_component | host cell synapse |
B | 0044231 | cellular_component | host cell presynaptic membrane |
B | 0046872 | molecular_function | metal ion binding |
B | 0071806 | biological_process | protein transmembrane transport |
B | 0090729 | molecular_function | toxin activity |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE ZN A1300 |
Chain | Residue |
A | HIS212 |
A | HIS216 |
A | GLU251 |
A | HOH1289 |
A | HOH1318 |
site_id | AC2 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE NA A1301 |
Chain | Residue |
A | HOH1317 |
A | ALA544 |
A | GLU547 |
A | GLN548 |
A | LYS550 |
site_id | AC3 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE NA A1302 |
Chain | Residue |
A | VAL593 |
A | ILE596 |
A | ALA597 |
A | ILE599 |
A | HOH1314 |
site_id | AC4 |
Number of Residues | 2 |
Details | BINDING SITE FOR RESIDUE ACT A1303 |
Chain | Residue |
A | TYR879 |
A | TYR1041 |
site_id | AC5 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE ZN B1300 |
Chain | Residue |
B | HIS212 |
B | HIS216 |
B | GLU251 |
B | HOH1275 |
B | HOH1284 |
site_id | AC6 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE NA B1302 |
Chain | Residue |
B | VAL593 |
B | ILE596 |
B | ILE599 |
B | SER600 |
B | HOH1283 |
site_id | AC7 |
Number of Residues | 2 |
Details | BINDING SITE FOR RESIDUE ACT B1303 |
Chain | Residue |
B | TYR879 |
B | TYR881 |
Functional Information from PROSITE/UniProt
site_id | PS00142 |
Number of Residues | 10 |
Details | ZINC_PROTEASE Neutral zinc metallopeptidases, zinc-binding region signature. TLMHELIHSL |
Chain | Residue | Details |
A | THR209-LEU218 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 98 |
Details | Region: {"description":"Belt","evidences":[{"source":"PubMed","id":"19118561","evidenceCode":"ECO:0000305"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI2 |
Number of Residues | 444 |
Details | Region: {"description":"N-terminus of receptor binding domain (N-RBD)","evidences":[{"source":"PubMed","id":"19118561","evidenceCode":"ECO:0000305"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI3 |
Number of Residues | 6 |
Details | Motif: {"description":"Host ganglioside-binding motif","evidences":[{"source":"UniProtKB","id":"P0DPI0","evidenceCode":"ECO:0000250"},{"source":"PubMed","id":"19650874","evidenceCode":"ECO:0000305"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI4 |
Number of Residues | 2 |
Details | Active site: {"description":"Proton acceptor","evidences":[{"source":"PROSITE-ProRule","id":"PRU10095","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"15157097","evidenceCode":"ECO:0000305"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI5 |
Number of Residues | 4 |
Details | Binding site: {"evidences":[{"source":"PROSITE-ProRule","id":"PRU10095","evidenceCode":"ECO:0000255"},{"source":"PDB","id":"1T3A","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1T3C","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1ZKW","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1ZKX","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1ZL6","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1ZN3","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3FFZ","evidenceCode":"ECO:0007744"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI6 |
Number of Residues | 2 |
Details | Binding site: {"evidences":[{"source":"PDB","id":"1T3A","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1T3C","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1ZKW","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1ZKX","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1ZL6","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1ZN3","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3FFZ","evidenceCode":"ECO:0007744"}]} |
Chain | Residue | Details |
Catalytic Information from CSA
site_id | CSA1 |
Number of Residues | 3 |
Details | Annotated By Reference To The Literature 1i1e |
Chain | Residue | Details |
A | ARG348 | |
A | GLU251 | |
A | TYR351 |
site_id | CSA2 |
Number of Residues | 3 |
Details | Annotated By Reference To The Literature 1i1e |
Chain | Residue | Details |
B | ARG348 | |
B | GLU251 | |
B | TYR351 |