4TSO
Crystal structure of FraC with DHPC bound (crystal form I)
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 | 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 | 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 PDB Data
| site_id | AC1 |
| Number of Residues | 9 |
| Details | binding site for residue HXG A 201 |
| Chain | Residue |
| A | ASN111 |
| A | TRP112 |
| A | TYR113 |
| A | TRP116 |
| A | TYR137 |
| A | HOH311 |
| A | HOH321 |
| B | PRO81 |
| B | HOH317 |
| site_id | AC2 |
| Number of Residues | 14 |
| Details | binding site for residue HXG A 202 |
| Chain | Residue |
| A | SER54 |
| A | ALA83 |
| A | GLY85 |
| A | SER105 |
| A | PRO107 |
| A | TYR108 |
| A | ASP109 |
| A | TYR113 |
| A | TYR133 |
| A | TYR137 |
| A | HXG203 |
| A | HOH310 |
| B | TRP112 |
| B | HXG201 |
| site_id | AC3 |
| Number of Residues | 6 |
| Details | binding site for residue HXG A 203 |
| Chain | Residue |
| A | ARG53 |
| A | GLN130 |
| A | TYR133 |
| A | GLU134 |
| A | TYR138 |
| A | HXG202 |
| site_id | AC4 |
| Number of Residues | 4 |
| Details | binding site for residue SO4 A 204 |
| Chain | Residue |
| A | LYS30 |
| A | ARG31 |
| B | ASN28 |
| B | ARG79 |
| site_id | AC5 |
| Number of Residues | 3 |
| Details | binding site for residue PO4 A 205 |
| Chain | Residue |
| A | ARG120 |
| A | TYR122 |
| A | LYS123 |
| site_id | AC6 |
| Number of Residues | 1 |
| Details | binding site for residue PO4 A 206 |
| Chain | Residue |
| A | HIS139 |
| site_id | AC7 |
| Number of Residues | 8 |
| Details | binding site for residue PO4 A 207 |
| Chain | Residue |
| A | ARG53 |
| A | GLY55 |
| A | ASN78 |
| A | VAL82 |
| A | THR84 |
| A | HOH345 |
| A | HOH346 |
| A | HOH348 |
| site_id | AC8 |
| Number of Residues | 18 |
| Details | binding site for residue HXG B 201 |
| Chain | Residue |
| A | TRP112 |
| A | HXG202 |
| B | SER54 |
| B | ALA83 |
| B | THR84 |
| B | GLY85 |
| B | SER105 |
| B | PRO107 |
| B | TYR108 |
| B | TRP112 |
| B | TYR113 |
| B | TYR133 |
| B | TYR137 |
| B | TYR138 |
| B | HXG202 |
| B | SO4203 |
| B | HOH329 |
| B | HOH361 |
| site_id | AC9 |
| Number of Residues | 6 |
| Details | binding site for residue HXG B 202 |
| Chain | Residue |
| B | TRP112 |
| B | TYR113 |
| B | TRP116 |
| B | TYR137 |
| B | HXG201 |
| B | HOH302 |
| site_id | AD1 |
| Number of Residues | 6 |
| Details | binding site for residue SO4 B 203 |
| Chain | Residue |
| B | ARG53 |
| B | GLN130 |
| B | TYR133 |
| B | TYR138 |
| B | HXG201 |
| B | HOH349 |
| site_id | AD2 |
| Number of Residues | 7 |
| Details | binding site for residue SO4 B 204 |
| Chain | Residue |
| A | TYR110 |
| B | VAL29 |
| B | LYS30 |
| B | LYS77 |
| B | ARG79 |
| B | GLY80 |
| B | HOH313 |
| site_id | AD3 |
| Number of Residues | 5 |
| Details | binding site for residue PO4 B 205 |
| Chain | Residue |
| B | ARG120 |
| B | VAL121 |
| B | TYR122 |
| B | LYS123 |
| B | TYR156 |
| site_id | AD4 |
| Number of Residues | 6 |
| Details | binding site for residue PO4 B 206 |
| Chain | Residue |
| B | HIS63 |
| B | HIS63 |
| B | HIS63 |
| B | LYS64 |
| B | LYS64 |
| B | LYS64 |
| site_id | AD5 |
| Number of Residues | 6 |
| Details | binding site for residue PO4 B 207 |
| Chain | Residue |
| B | LYS30 |
| B | LYS30 |
| B | ARG31 |
| B | ARG31 |
| B | HIS169 |
| B | HIS169 |
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 |
