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 | 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 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 | 4 |
Details | BINDING: in subunit A; in oligomeric forms only => ECO:0000305|PubMed:25716479 |
Chain | Residue | Details |
A | ARG31 | |
A | GLY168 | |
B | ARG31 | |
B | GLY168 |
site_id | SWS_FT_FI2 |
Number of Residues | 6 |
Details | BINDING: BINDING => ECO:0000269|PubMed:28630155 |
Chain | Residue | Details |
A | TYR51 | |
A | ARG53 | |
A | TYR138 | |
B | TYR51 | |
B | ARG53 | |
B | TYR138 |
site_id | SWS_FT_FI3 |
Number of Residues | 18 |
Details | BINDING: in monomeric and oligomeric forms => ECO:0000305|PubMed:25716479 |
Chain | Residue | Details |
A | SER54 | |
B | SER54 | |
B | GLY85 | |
B | TYR108 | |
B | TYR113 | |
B | SER114 | |
B | TRP116 | |
B | TYR133 | |
B | TYR137 | |
B | ARG144 | |
A | GLY85 | |
A | TYR108 | |
A | TYR113 | |
A | SER114 | |
A | TRP116 | |
A | TYR133 | |
A | TYR137 | |
A | ARG144 |
site_id | SWS_FT_FI4 |
Number of Residues | 2 |
Details | BINDING: in subunit B; in oligomeric forms only => ECO:0000305|PubMed:25716479 |
Chain | Residue | Details |
A | ARG79 | |
B | ARG79 |
site_id | SWS_FT_FI5 |
Number of Residues | 2 |
Details | SITE: 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) => ECO:0000305|PubMed:21300287, ECO:0000305|PubMed:25716479, ECO:0000305|PubMed:25759390 |
Chain | Residue | Details |
A | PHE16 | |
B | PHE16 |
site_id | SWS_FT_FI6 |
Number of Residues | 2 |
Details | SITE: Protrudes from one subunit (B) and inserts into the hydrophobic cavity from the adjacent subunit (A) => ECO:0000305|PubMed:21300287, ECO:0000305|PubMed:25716479 |
Chain | Residue | Details |
A | VAL60 | |
B | VAL60 |
site_id | SWS_FT_FI7 |
Number of Residues | 2 |
Details | SITE: Part of the hydrophobic cavity (in subunit A) that receives Val-60 from the adjacent subunit (B) => ECO:0000305|PubMed:21300287, ECO:0000305|PubMed:25716479 |
Chain | Residue | Details |
A | TRP149 | |
B | TRP149 |
site_id | SWS_FT_FI8 |
Number of Residues | 2 |
Details | SITE: Part of the hydrophobic cavity (in subunit A) that receives Val-60 from the adjacent subunit (B) => ECO:0000305|PubMed:21300287 |
Chain | Residue | Details |
A | PHE163 | |
B | PHE163 |