4TSL
Crystal structure of FraC with POC 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 | 15 |
| Details | binding site for residue PC A 201 |
| Chain | Residue |
| A | ARG53 |
| A | TYR138 |
| A | FMT203 |
| A | HOH310 |
| A | HOH360 |
| B | TYR138 |
| B | SO4203 |
| A | SER54 |
| A | GLY85 |
| A | SER105 |
| A | PRO107 |
| A | TYR108 |
| A | TYR113 |
| A | TYR133 |
| A | TYR137 |
| site_id | AC2 |
| Number of Residues | 14 |
| Details | binding site for residue PC A 202 |
| Chain | Residue |
| A | TRP112 |
| A | TYR113 |
| A | SER114 |
| A | TRP116 |
| A | TYR137 |
| A | PRO142 |
| A | FMT206 |
| A | HOH301 |
| A | HOH306 |
| A | HOH314 |
| A | HOH367 |
| B | TRP112 |
| B | TYR113 |
| B | HOH317 |
| site_id | AC3 |
| Number of Residues | 5 |
| Details | binding site for residue FMT A 203 |
| Chain | Residue |
| A | ARG53 |
| A | SER54 |
| A | PC201 |
| B | GLU134 |
| B | TYR138 |
| site_id | AC4 |
| Number of Residues | 4 |
| Details | binding site for residue FMT A 204 |
| Chain | Residue |
| A | HIS63 |
| A | LYS64 |
| A | HOH353 |
| B | ARG161 |
| site_id | AC5 |
| Number of Residues | 4 |
| Details | binding site for residue FMT A 205 |
| Chain | Residue |
| A | LEU23 |
| A | LYS32 |
| A | HIS169 |
| A | HOH313 |
| site_id | AC6 |
| Number of Residues | 7 |
| Details | binding site for residue FMT A 206 |
| Chain | Residue |
| A | TYR113 |
| A | SER114 |
| A | TRP116 |
| A | TYR137 |
| A | PC202 |
| A | HOH367 |
| B | TYR113 |
| site_id | AC7 |
| Number of Residues | 5 |
| Details | binding site for residue FMT A 207 |
| Chain | Residue |
| A | ARG120 |
| A | TYR122 |
| A | LYS123 |
| A | HOH403 |
| A | HOH405 |
| site_id | AC8 |
| Number of Residues | 7 |
| Details | binding site for residue GOL A 208 |
| Chain | Residue |
| A | ALA2 |
| A | ASP3 |
| A | VAL18 |
| A | HOH302 |
| A | HOH318 |
| A | HOH425 |
| B | ASP58 |
| site_id | AC9 |
| Number of Residues | 5 |
| Details | binding site for residue ACT A 209 |
| Chain | Residue |
| A | ASN147 |
| A | ASN165 |
| A | SER166 |
| A | SER167 |
| A | HOH423 |
| site_id | AD1 |
| Number of Residues | 14 |
| Details | binding site for residue PC B 201 |
| Chain | Residue |
| A | TYR138 |
| B | ARG53 |
| B | SER54 |
| B | GLY85 |
| B | SER105 |
| B | PRO107 |
| B | TYR108 |
| B | TYR113 |
| B | TYR133 |
| B | TYR137 |
| B | TYR138 |
| B | FMT206 |
| B | HOH309 |
| B | HOH374 |
| site_id | AD2 |
| Number of Residues | 9 |
| Details | binding site for residue PC B 202 |
| Chain | Residue |
| A | TRP112 |
| A | TYR113 |
| B | TRP116 |
| B | TYR137 |
| B | TYR138 |
| B | PRO142 |
| B | HOH301 |
| B | HOH440 |
| B | HOH455 |
| site_id | AD3 |
| Number of Residues | 9 |
| Details | binding site for residue SO4 B 203 |
| Chain | Residue |
| A | ARG53 |
| A | GLN130 |
| A | TYR133 |
| A | TYR138 |
| A | PC201 |
| B | ARG53 |
| B | GLN130 |
| B | TYR133 |
| B | TYR138 |
| site_id | AD4 |
| Number of Residues | 6 |
| Details | binding site for residue SO4 B 204 |
| Chain | Residue |
| B | LYS30 |
| B | LYS77 |
| B | ARG79 |
| B | GLY80 |
| B | HOH473 |
| B | VAL29 |
| site_id | AD5 |
| Number of Residues | 6 |
| Details | binding site for residue FMT B 205 |
| Chain | Residue |
| A | TRP112 |
| A | TYR113 |
| B | TYR113 |
| B | SER114 |
| B | TRP116 |
| B | TYR137 |
| site_id | AD6 |
| Number of Residues | 5 |
| Details | binding site for residue FMT B 206 |
| Chain | Residue |
| A | TYR138 |
| A | HIS139 |
| B | ARG53 |
| B | THR84 |
| B | PC201 |
| site_id | AD7 |
| Number of Residues | 4 |
| Details | binding site for residue FMT B 207 |
| Chain | Residue |
| A | HIS63 |
| B | HIS150 |
| B | SER151 |
| B | HOH373 |
| site_id | AD8 |
| Number of Residues | 5 |
| Details | binding site for residue FMT B 208 |
| Chain | Residue |
| A | ARG79 |
| B | ASN28 |
| B | LYS30 |
| B | HIS169 |
| B | HOH472 |
| site_id | AD9 |
| Number of Residues | 5 |
| Details | binding site for residue FMT B 209 |
| Chain | Residue |
| B | ARG120 |
| B | TYR122 |
| B | LYS123 |
| B | HOH417 |
| B | HOH484 |
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 |
