6K2G
Structure of FraE in the monomer state
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0005576 | cellular_component | extracellular region |
| A | 0006811 | biological_process | monoatomic ion transport |
| A | 0006812 | biological_process | monoatomic cation transport |
| A | 0008289 | molecular_function | lipid binding |
| A | 0015267 | molecular_function | channel activity |
| A | 0016020 | cellular_component | membrane |
| A | 0031640 | biological_process | killing of cells of another organism |
| A | 0035821 | biological_process | modulation of process of another organism |
| A | 0042151 | cellular_component | nematocyst |
| A | 0042802 | molecular_function | identical protein binding |
| A | 0044218 | cellular_component | other organism cell membrane |
| A | 0046930 | cellular_component | pore complex |
| A | 0046931 | biological_process | pore complex assembly |
| A | 0051715 | biological_process | cytolysis in another organism |
| A | 0055085 | biological_process | transmembrane transport |
| A | 0090729 | molecular_function | toxin activity |
| B | 0005576 | cellular_component | extracellular region |
| B | 0006811 | biological_process | monoatomic ion transport |
| B | 0006812 | biological_process | monoatomic cation transport |
| B | 0008289 | molecular_function | lipid binding |
| B | 0015267 | molecular_function | channel activity |
| B | 0016020 | cellular_component | membrane |
| B | 0031640 | biological_process | killing of cells of another organism |
| B | 0035821 | biological_process | modulation of process of another organism |
| B | 0042151 | cellular_component | nematocyst |
| B | 0042802 | molecular_function | identical protein binding |
| B | 0044218 | cellular_component | other organism cell membrane |
| B | 0046930 | cellular_component | pore complex |
| B | 0046931 | biological_process | pore complex assembly |
| B | 0051715 | biological_process | cytolysis in another organism |
| B | 0055085 | biological_process | transmembrane transport |
| B | 0090729 | molecular_function | toxin activity |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 30 |
| Details | Region: {"description":"Trp-rich region, which is important for the binding to lipid membrane","evidences":[{"source":"UniProtKB","id":"P61914","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 4 |
| Details | Motif: {"description":"Cell attachment site, crucial for protein stability","evidences":[{"source":"UniProtKB","id":"P07845","evidenceCode":"ECO:0000250"},{"evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 4 |
| Details | Binding site: {"description":"in subunit A; in oligomeric forms only","evidences":[{"source":"PubMed","id":"25716479","evidenceCode":"ECO:0000305"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 6 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"28630155","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI5 |
| Number of Residues | 18 |
| Details | Binding site: {"description":"in monomeric and oligomeric forms","evidences":[{"source":"PubMed","id":"25716479","evidenceCode":"ECO:0000305"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI6 |
| Number of Residues | 2 |
| Details | Binding site: {"description":"in subunit B; in oligomeric forms only","evidences":[{"source":"PubMed","id":"25716479","evidenceCode":"ECO:0000305"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI7 |
| Number of Residues | 2 |
| Details | Site: {"description":"Part of the hydrophobic cavity (in subunit A) that receives Val-60 from the adjacent subunit (B); essential in hemolysis, since it is critical for pore formation in cholesterol-rich membrane cells (such as red blood cells)","evidences":[{"source":"PubMed","id":"21300287","evidenceCode":"ECO:0000305"},{"source":"PubMed","id":"25716479","evidenceCode":"ECO:0000305"},{"source":"PubMed","id":"25759390","evidenceCode":"ECO:0000305"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI8 |
| Number of Residues | 2 |
| Details | Site: {"description":"Protrudes from one subunit (B) and inserts into the hydrophobic cavity from the adjacent subunit (A)","evidences":[{"source":"PubMed","id":"21300287","evidenceCode":"ECO:0000305"},{"source":"PubMed","id":"25716479","evidenceCode":"ECO:0000305"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI9 |
| Number of Residues | 2 |
| Details | Site: {"description":"Part of the hydrophobic cavity (in subunit A) that receives Val-60 from the adjacent subunit (B)","evidences":[{"source":"PubMed","id":"21300287","evidenceCode":"ECO:0000305"},{"source":"PubMed","id":"25716479","evidenceCode":"ECO:0000305"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI10 |
| Number of Residues | 2 |
| Details | Site: {"description":"Part of the hydrophobic cavity (in subunit A) that receives Val-60 from the adjacent subunit (B)","evidences":[{"source":"PubMed","id":"21300287","evidenceCode":"ECO:0000305"}]} |
| Chain | Residue | Details |
