4TSN
Crystal structure of FraC with POC bound (crystal form II)
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 |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 13 |
Details | binding site for residue PC A 201 |
Chain | Residue |
A | SER54 |
A | TYR138 |
A | HOH303 |
A | HOH318 |
A | HOH348 |
A | THR84 |
A | GLY85 |
A | SER105 |
A | PRO107 |
A | TYR108 |
A | TYR113 |
A | TYR133 |
A | TYR137 |
site_id | AC2 |
Number of Residues | 7 |
Details | binding site for residue PC A 202 |
Chain | Residue |
A | TYR113 |
A | SER114 |
A | TRP116 |
A | TYR137 |
A | PRO142 |
A | GOL206 |
A | HOH304 |
site_id | AC3 |
Number of Residues | 2 |
Details | binding site for residue PC A 203 |
Chain | Residue |
A | TRP112 |
A | TYR113 |
site_id | AC4 |
Number of Residues | 5 |
Details | binding site for residue SO4 A 204 |
Chain | Residue |
A | ARG120 |
A | TYR122 |
A | LYS123 |
A | HOH366 |
A | HOH401 |
site_id | AC5 |
Number of Residues | 5 |
Details | binding site for residue SO4 A 205 |
Chain | Residue |
A | LYS30 |
A | ARG31 |
A | HOH305 |
A | HOH377 |
A | HOH454 |
site_id | AC6 |
Number of Residues | 6 |
Details | binding site for residue GOL A 206 |
Chain | Residue |
A | TRP112 |
A | TYR113 |
A | SER114 |
A | ARG144 |
A | PC202 |
A | HOH302 |
site_id | AC7 |
Number of Residues | 14 |
Details | binding site for residue PC B 201 |
Chain | Residue |
B | ARG53 |
B | SER54 |
B | THR84 |
B | GLY85 |
B | SER105 |
B | PRO107 |
B | TYR108 |
B | TYR113 |
B | TYR133 |
B | TYR137 |
B | TYR138 |
B | HOH302 |
B | HOH325 |
B | HOH352 |
site_id | AC8 |
Number of Residues | 6 |
Details | binding site for residue PC B 202 |
Chain | Residue |
B | TYR113 |
B | SER114 |
B | TRP116 |
B | TYR137 |
B | HOH311 |
B | HOH394 |
site_id | AC9 |
Number of Residues | 8 |
Details | binding site for residue SO4 B 203 |
Chain | Residue |
A | LYS30 |
A | TYR108 |
A | HOH307 |
B | ARG120 |
B | TYR122 |
B | LYS123 |
B | HOH303 |
B | HOH313 |
site_id | AD1 |
Number of Residues | 4 |
Details | binding site for residue SO4 B 204 |
Chain | Residue |
B | ARG144 |
B | HOH439 |
D | GLY124 |
D | GLN125 |
site_id | AD2 |
Number of Residues | 3 |
Details | binding site for residue ACT B 205 |
Chain | Residue |
A | ASP109 |
A | TRP112 |
B | LYS123 |
site_id | AD3 |
Number of Residues | 14 |
Details | binding site for residue PC C 201 |
Chain | Residue |
C | ARG53 |
C | SER54 |
C | GLY85 |
C | SER105 |
C | PRO107 |
C | TYR108 |
C | TYR113 |
C | TYR133 |
C | TYR137 |
C | TYR138 |
C | SO4202 |
C | HOH301 |
C | HOH311 |
C | HOH351 |
site_id | AD4 |
Number of Residues | 5 |
Details | binding site for residue SO4 C 202 |
Chain | Residue |
C | ARG53 |
C | GLN130 |
C | TYR133 |
C | TYR138 |
C | PC201 |
site_id | AD5 |
Number of Residues | 9 |
Details | binding site for residue SO4 C 203 |
Chain | Residue |
C | HOH377 |
D | HOH334 |
C | VAL29 |
C | LYS30 |
C | LYS77 |
C | ARG79 |
C | GLY80 |
C | HOH303 |
C | HOH306 |
site_id | AD6 |
Number of Residues | 5 |
Details | binding site for residue SO4 C 204 |
Chain | Residue |
C | ARG120 |
C | TYR122 |
C | LYS123 |
C | HOH413 |
C | HOH441 |
site_id | AD7 |
Number of Residues | 14 |
Details | binding site for residue PC D 201 |
Chain | Residue |
D | ARG53 |
D | SER54 |
D | GLY85 |
D | SER105 |
D | PRO107 |
D | TYR108 |
D | TYR113 |
D | TYR133 |
D | TYR137 |
D | TYR138 |
D | SO4203 |
D | HOH304 |
D | HOH330 |
D | HOH372 |
site_id | AD8 |
Number of Residues | 7 |
Details | binding site for residue PC D 202 |
Chain | Residue |
D | TRP112 |
D | TYR113 |
D | SER114 |
D | TRP116 |
D | TYR137 |
D | PRO142 |
D | HOH390 |
site_id | AD9 |
Number of Residues | 5 |
Details | binding site for residue SO4 D 203 |
Chain | Residue |
D | ARG53 |
D | GLN130 |
D | TYR133 |
D | TYR138 |
D | PC201 |
site_id | AE1 |
Number of Residues | 8 |
Details | binding site for residue SO4 D 204 |
Chain | Residue |
D | ASN28 |
D | VAL29 |
D | LYS30 |
D | LYS77 |
D | ARG79 |
D | GLY80 |
D | HOH337 |
D | HOH343 |
site_id | AE2 |
Number of Residues | 6 |
Details | binding site for residue SO4 D 205 |
Chain | Residue |
B | THR56 |
B | ASN78 |
B | ARG79 |
D | SER167 |
D | HOH318 |
D | HOH336 |
site_id | AE3 |
Number of Residues | 5 |
Details | binding site for residue SO4 D 206 |
Chain | Residue |
C | ARG79 |
D | ARG120 |
D | TYR122 |
D | LYS123 |
D | HOH405 |
site_id | AE4 |
Number of Residues | 1 |
Details | binding site for residue SO4 D 207 |
Chain | Residue |
D | LYS178 |
site_id | AE5 |
Number of Residues | 2 |
Details | binding site for residue ACT D 208 |
Chain | Residue |
D | ASN28 |
D | ARG79 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 8 |
Details | BINDING: in subunit A; in oligomeric forms only => ECO:0000305|PubMed:25716479 |
Chain | Residue | Details |
A | ARG31 | |
A | GLY168 | |
B | ARG31 | |
B | GLY168 | |
C | ARG31 | |
C | GLY168 | |
D | ARG31 | |
D | GLY168 |
site_id | SWS_FT_FI2 |
Number of Residues | 12 |
Details | BINDING: BINDING => ECO:0000269|PubMed:28630155 |
Chain | Residue | Details |
A | TYR51 | |
D | TYR51 | |
D | ARG53 | |
D | 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 | 36 |
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 | |
A | TYR113 | |
A | SER114 | |
A | TRP116 | |
A | TYR133 | |
A | TYR137 | |
A | ARG144 |
site_id | SWS_FT_FI4 |
Number of Residues | 4 |
Details | BINDING: in subunit B; in oligomeric forms only => ECO:0000305|PubMed:25716479 |
Chain | Residue | Details |
A | ARG79 | |
B | ARG79 | |
C | ARG79 | |
D | ARG79 |
site_id | SWS_FT_FI5 |
Number of Residues | 4 |
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 |
site_id | SWS_FT_FI6 |
Number of Residues | 4 |
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 |
site_id | SWS_FT_FI7 |
Number of Residues | 4 |
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 |
site_id | SWS_FT_FI8 |
Number of Residues | 4 |
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 |