4TSQ
Crystal structure of FraC with DHPC bound (crystal form III)
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 |
C | 0005576 | cellular_component | extracellular region |
C | 0006811 | biological_process | monoatomic ion transport |
C | 0006812 | biological_process | monoatomic cation transport |
C | 0008289 | molecular_function | lipid binding |
C | 0015267 | molecular_function | channel activity |
C | 0016020 | cellular_component | membrane |
C | 0031640 | biological_process | killing of cells of another organism |
C | 0035821 | biological_process | modulation of process of another organism |
C | 0042151 | cellular_component | nematocyst |
C | 0042802 | molecular_function | identical protein binding |
C | 0044218 | cellular_component | other organism cell membrane |
C | 0046930 | cellular_component | pore complex |
C | 0046931 | biological_process | pore complex assembly |
C | 0051715 | biological_process | cytolysis in another organism |
C | 0055085 | biological_process | transmembrane transport |
C | 0090729 | molecular_function | toxin activity |
D | 0005576 | cellular_component | extracellular region |
D | 0006811 | biological_process | monoatomic ion transport |
D | 0006812 | biological_process | monoatomic cation transport |
D | 0008289 | molecular_function | lipid binding |
D | 0015267 | molecular_function | channel activity |
D | 0016020 | cellular_component | membrane |
D | 0031640 | biological_process | killing of cells of another organism |
D | 0035821 | biological_process | modulation of process of another organism |
D | 0042151 | cellular_component | nematocyst |
D | 0042802 | molecular_function | identical protein binding |
D | 0044218 | cellular_component | other organism cell membrane |
D | 0046930 | cellular_component | pore complex |
D | 0046931 | biological_process | pore complex assembly |
D | 0051715 | biological_process | cytolysis in another organism |
D | 0055085 | biological_process | transmembrane transport |
D | 0090729 | molecular_function | toxin activity |
E | 0005576 | cellular_component | extracellular region |
E | 0006811 | biological_process | monoatomic ion transport |
E | 0006812 | biological_process | monoatomic cation transport |
E | 0008289 | molecular_function | lipid binding |
E | 0015267 | molecular_function | channel activity |
E | 0016020 | cellular_component | membrane |
E | 0031640 | biological_process | killing of cells of another organism |
E | 0035821 | biological_process | modulation of process of another organism |
E | 0042151 | cellular_component | nematocyst |
E | 0042802 | molecular_function | identical protein binding |
E | 0044218 | cellular_component | other organism cell membrane |
E | 0046930 | cellular_component | pore complex |
E | 0046931 | biological_process | pore complex assembly |
E | 0051715 | biological_process | cytolysis in another organism |
E | 0055085 | biological_process | transmembrane transport |
E | 0090729 | molecular_function | toxin activity |
F | 0005576 | cellular_component | extracellular region |
F | 0006811 | biological_process | monoatomic ion transport |
F | 0006812 | biological_process | monoatomic cation transport |
F | 0008289 | molecular_function | lipid binding |
F | 0015267 | molecular_function | channel activity |
F | 0016020 | cellular_component | membrane |
F | 0031640 | biological_process | killing of cells of another organism |
F | 0035821 | biological_process | modulation of process of another organism |
F | 0042151 | cellular_component | nematocyst |
F | 0042802 | molecular_function | identical protein binding |
F | 0044218 | cellular_component | other organism cell membrane |
F | 0046930 | cellular_component | pore complex |
F | 0046931 | biological_process | pore complex assembly |
F | 0051715 | biological_process | cytolysis in another organism |
F | 0055085 | biological_process | transmembrane transport |
F | 0090729 | molecular_function | toxin activity |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 16 |
Details | binding site for residue HXG A 201 |
Chain | Residue |
A | ARG53 |
A | TYR113 |
A | TYR133 |
A | TYR137 |
A | HXG203 |
A | HOH366 |
A | HOH425 |
A | HOH440 |
A | SER54 |
A | THR84 |
A | GLY85 |
A | VAL87 |
A | SER105 |
A | PRO107 |
A | TYR108 |
A | TRP112 |
site_id | AC2 |
Number of Residues | 9 |
Details | binding site for residue HXG A 202 |
Chain | Residue |
A | TRP112 |
A | TYR113 |
A | TRP116 |
A | TYR137 |
A | TYR138 |
A | HXG204 |
A | HOH382 |
A | HOH407 |
A | HOH466 |
site_id | AC3 |
Number of Residues | 7 |
Details | binding site for residue HXG A 203 |
Chain | Residue |
A | ARG53 |
A | GLN130 |
A | TYR133 |
A | GLU134 |
A | TYR138 |
A | HXG201 |
A | PC207 |
site_id | AC4 |
Number of Residues | 8 |
Details | binding site for residue HXG A 204 |
Chain | Residue |
A | ASN111 |
A | TRP112 |
A | SER114 |
A | ARG144 |
A | HXG202 |
A | PC207 |
A | HOH382 |
A | HOH460 |
site_id | AC5 |
Number of Residues | 17 |
Details | binding site for residue HXG A 205 |
Chain | Residue |
A | VAL121 |
A | TYR122 |
A | LYS123 |
A | ARG140 |
A | LEU154 |
A | TYR156 |
A | HOH410 |
A | HOH420 |
E | ILE9 |
E | ASP17 |
E | VAL18 |
E | THR21 |
E | VAL22 |
E | ALA25 |
E | ILE59 |
E | LEU72 |
E | HOH357 |
site_id | AC6 |
Number of Residues | 9 |
Details | binding site for residue PC A 206 |
Chain | Residue |
A | ASN78 |
A | VAL82 |
A | THR84 |
A | HOH392 |
A | HOH440 |
F | ASN111 |
F | TRP112 |
F | TYR113 |
F | SER114 |
site_id | AC7 |
Number of Residues | 4 |
Details | binding site for residue PC A 207 |
Chain | Residue |
A | TYR138 |
A | HIS139 |
A | HXG203 |
A | HXG204 |
site_id | AC8 |
Number of Residues | 5 |
Details | binding site for residue SCN A 208 |
Chain | Residue |
A | LYS43 |
A | MET94 |
A | ASP96 |
A | GLY97 |
A | ASN98 |
site_id | AC9 |
Number of Residues | 10 |
Details | binding site for residue HXG B 201 |
Chain | Residue |
B | TRP112 |
B | TYR113 |
B | TRP116 |
B | TYR137 |
B | TYR138 |
B | HXG202 |
B | HXG204 |
B | HOH355 |
B | HOH400 |
B | HOH407 |
site_id | AD1 |
Number of Residues | 15 |
Details | binding site for residue HXG B 202 |
Chain | Residue |
B | HOH383 |
B | ARG53 |
B | SER54 |
B | THR84 |
B | GLY85 |
B | VAL87 |
B | SER105 |
B | PRO107 |
B | TYR108 |
B | TYR113 |
B | TYR133 |
B | TYR137 |
B | TYR138 |
B | HXG201 |
B | HXG203 |
site_id | AD2 |
Number of Residues | 8 |
Details | binding site for residue HXG B 203 |
Chain | Residue |
B | ARG53 |
B | GLN130 |
B | TYR133 |
B | GLU134 |
B | TYR138 |
B | HXG202 |
B | HXG204 |
B | CL206 |
site_id | AD3 |
Number of Residues | 8 |
Details | binding site for residue HXG B 204 |
Chain | Residue |
B | ASN111 |
B | TRP112 |
B | SER114 |
B | ARG144 |
B | HXG201 |
B | HXG203 |
B | HOH355 |
E | HXG201 |
site_id | AD4 |
Number of Residues | 6 |
Details | binding site for residue SCN B 205 |
Chain | Residue |
B | LYS43 |
B | MET94 |
B | ASP96 |
B | GLY97 |
B | ASN98 |
B | TYR156 |
site_id | AD5 |
Number of Residues | 2 |
Details | binding site for residue CL B 206 |
Chain | Residue |
B | HIS139 |
B | HXG203 |
site_id | AD6 |
Number of Residues | 7 |
Details | binding site for residue HXG C 201 |
Chain | Residue |
C | TRP112 |
C | TYR113 |
C | SER114 |
C | TRP116 |
C | TYR137 |
C | HOH393 |
C | HOH409 |
site_id | AD7 |
Number of Residues | 14 |
Details | binding site for residue HXG C 202 |
Chain | Residue |
C | ARG53 |
C | SER54 |
C | THR84 |
C | GLY85 |
C | VAL87 |
C | SER105 |
C | PRO107 |
C | TYR108 |
C | TYR113 |
C | TYR133 |
C | TYR137 |
C | TYR138 |
C | PC203 |
C | HOH363 |
site_id | AD8 |
Number of Residues | 6 |
Details | binding site for residue PC C 203 |
Chain | Residue |
C | ARG53 |
C | GLN130 |
C | TYR133 |
C | TYR138 |
C | HXG202 |
D | ARG53 |
site_id | AD9 |
Number of Residues | 8 |
Details | binding site for residue HXG D 201 |
Chain | Residue |
D | TRP112 |
D | TYR113 |
D | SER114 |
D | TRP116 |
D | TYR137 |
D | TYR138 |
D | HOH400 |
D | HOH405 |
site_id | AE1 |
Number of Residues | 14 |
Details | binding site for residue HXG D 202 |
Chain | Residue |
D | SER54 |
D | ALA83 |
D | THR84 |
D | GLY85 |
D | VAL87 |
D | SER105 |
D | PRO107 |
D | TYR108 |
D | TYR113 |
D | TYR133 |
D | TYR137 |
D | PC203 |
D | HOH366 |
D | HOH404 |
site_id | AE2 |
Number of Residues | 6 |
Details | binding site for residue PC D 203 |
Chain | Residue |
D | ARG53 |
D | TYR133 |
D | GLU134 |
D | TYR138 |
D | HXG202 |
D | HOH404 |
site_id | AE3 |
Number of Residues | 6 |
Details | binding site for residue SCN D 204 |
Chain | Residue |
D | LYS43 |
D | MET94 |
D | ASP96 |
D | GLY97 |
D | ASN98 |
D | TYR156 |
site_id | AE4 |
Number of Residues | 8 |
Details | binding site for residue HXG E 201 |
Chain | Residue |
B | HXG204 |
E | TRP112 |
E | TYR113 |
E | TRP116 |
E | TYR137 |
E | PC203 |
E | HOH345 |
E | HOH385 |
site_id | AE5 |
Number of Residues | 13 |
Details | binding site for residue HXG E 202 |
Chain | Residue |
E | SER54 |
E | ALA83 |
E | THR84 |
E | GLY85 |
E | VAL87 |
E | SER105 |
E | PRO107 |
E | TYR108 |
E | TYR113 |
E | TYR133 |
E | TYR137 |
E | PC204 |
E | HOH354 |
site_id | AE6 |
Number of Residues | 8 |
Details | binding site for residue PC E 203 |
Chain | Residue |
D | LYS64 |
E | ASN111 |
E | TRP112 |
E | SER114 |
E | ARG144 |
E | HXG201 |
E | HOH345 |
E | HOH355 |
site_id | AE7 |
Number of Residues | 6 |
Details | binding site for residue PC E 204 |
Chain | Residue |
E | ARG53 |
E | GLN130 |
E | TYR133 |
E | GLU134 |
E | TYR138 |
E | HXG202 |
site_id | AE8 |
Number of Residues | 5 |
Details | binding site for residue SCN E 205 |
Chain | Residue |
E | LYS43 |
E | MET94 |
E | ASP96 |
E | GLY97 |
E | ASN98 |
site_id | AE9 |
Number of Residues | 6 |
Details | binding site for residue HXG F 201 |
Chain | Residue |
F | TRP112 |
F | TYR113 |
F | SER114 |
F | TRP116 |
F | TYR137 |
F | TYR138 |
site_id | AF1 |
Number of Residues | 11 |
Details | binding site for residue PC F 202 |
Chain | Residue |
F | SER54 |
F | GLY85 |
F | VAL87 |
F | SER105 |
F | PRO107 |
F | TYR108 |
F | TYR113 |
F | TYR133 |
F | TYR137 |
F | PC203 |
F | HOH359 |
site_id | AF2 |
Number of Residues | 6 |
Details | binding site for residue PC F 203 |
Chain | Residue |
F | ARG53 |
F | TYR113 |
F | GLN130 |
F | TYR133 |
F | TYR138 |
F | PC202 |
site_id | AF3 |
Number of Residues | 7 |
Details | binding site for residue SCN F 204 |
Chain | Residue |
B | TRP149 |
B | HIS150 |
B | SER151 |
B | ARG161 |
F | PHE16 |
F | ASP17 |
F | HOH304 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 12 |
Details | BINDING: in subunit A; in oligomeric forms only => ECO:0000305|PubMed:25716479 |
Chain | Residue | Details |
A | ARG31 | |
E | GLY168 | |
F | ARG31 | |
F | GLY168 | |
A | GLY168 | |
B | ARG31 | |
B | GLY168 | |
C | ARG31 | |
C | GLY168 | |
D | ARG31 | |
D | GLY168 | |
E | ARG31 |
site_id | SWS_FT_FI2 |
Number of Residues | 18 |
Details | BINDING: BINDING => ECO:0000269|PubMed:28630155 |
Chain | Residue | Details |
A | TYR51 | |
D | TYR51 | |
D | ARG53 | |
D | TYR138 | |
E | TYR51 | |
E | ARG53 | |
E | TYR138 | |
F | TYR51 | |
F | ARG53 | |
F | TYR138 | |
A | ARG53 | |
A | TYR138 | |
B | TYR51 | |
B | ARG53 | |
B | TYR138 | |
C | TYR51 | |
C | ARG53 | |
C | TYR138 |
site_id | SWS_FT_FI3 |
Number of Residues | 54 |
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 | |
C | SER54 | |
A | GLY85 | |
C | GLY85 | |
C | TYR108 | |
C | TYR113 | |
C | SER114 | |
C | TRP116 | |
C | TYR133 | |
C | TYR137 | |
C | ARG144 | |
D | SER54 | |
D | GLY85 | |
A | TYR108 | |
D | TYR108 | |
D | TYR113 | |
D | SER114 | |
D | TRP116 | |
D | TYR133 | |
D | TYR137 | |
D | ARG144 | |
E | SER54 | |
E | GLY85 | |
E | TYR108 | |
A | TYR113 | |
E | TYR113 | |
E | SER114 | |
E | TRP116 | |
E | TYR133 | |
E | TYR137 | |
E | ARG144 | |
F | SER54 | |
F | GLY85 | |
F | TYR108 | |
F | TYR113 | |
A | SER114 | |
F | SER114 | |
F | TRP116 | |
F | TYR133 | |
F | TYR137 | |
F | ARG144 | |
A | TRP116 | |
A | TYR133 | |
A | TYR137 | |
A | ARG144 |
site_id | SWS_FT_FI4 |
Number of Residues | 6 |
Details | BINDING: in subunit B; in oligomeric forms only => ECO:0000305|PubMed:25716479 |
Chain | Residue | Details |
A | ARG79 | |
B | ARG79 | |
C | ARG79 | |
D | ARG79 | |
E | ARG79 | |
F | ARG79 |
site_id | SWS_FT_FI5 |
Number of Residues | 6 |
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 | |
C | PHE16 | |
D | PHE16 | |
E | PHE16 | |
F | PHE16 |
site_id | SWS_FT_FI6 |
Number of Residues | 6 |
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 | |
C | VAL60 | |
D | VAL60 | |
E | VAL60 | |
F | VAL60 |
site_id | SWS_FT_FI7 |
Number of Residues | 6 |
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 | |
C | TRP149 | |
D | TRP149 | |
E | TRP149 | |
F | TRP149 |
site_id | SWS_FT_FI8 |
Number of Residues | 6 |
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 | |
C | PHE163 | |
D | PHE163 | |
E | PHE163 | |
F | PHE163 |