4TSY
Crystal structure of FraC with lipids
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 | 10 |
| Details | binding site for residue HXJ A 201 |
| Chain | Residue |
| A | ARG53 |
| A | SO4204 |
| A | SER54 |
| A | THR84 |
| A | GLY85 |
| A | PRO107 |
| A | TYR108 |
| A | TYR113 |
| A | TYR133 |
| A | TYR137 |
| site_id | AC2 |
| Number of Residues | 7 |
| Details | binding site for residue HXJ A 202 |
| Chain | Residue |
| A | ASN111 |
| A | TRP112 |
| A | TYR113 |
| A | SER114 |
| A | TRP116 |
| A | TYR137 |
| A | PRO142 |
| site_id | AC3 |
| Number of Residues | 3 |
| Details | binding site for residue SO4 A 203 |
| Chain | Residue |
| A | ARG120 |
| A | TYR122 |
| A | LYS123 |
| site_id | AC4 |
| Number of Residues | 5 |
| Details | binding site for residue SO4 A 204 |
| Chain | Residue |
| A | ARG53 |
| A | GLN130 |
| A | TYR133 |
| A | TYR138 |
| A | HXJ201 |
| site_id | AC5 |
| Number of Residues | 4 |
| Details | binding site for residue SO4 A 205 |
| Chain | Residue |
| A | TRP149 |
| A | ARG161 |
| A | HIS175 |
| B | HIS63 |
| site_id | AC6 |
| Number of Residues | 4 |
| Details | binding site for residue SO4 A 206 |
| Chain | Residue |
| A | THR44 |
| A | SER95 |
| A | HTO209 |
| C | LYS123 |
| site_id | AC7 |
| Number of Residues | 2 |
| Details | binding site for residue SO4 A 207 |
| Chain | Residue |
| A | ARG79 |
| D | HIS169 |
| site_id | AC8 |
| Number of Residues | 2 |
| Details | binding site for residue SO4 A 208 |
| Chain | Residue |
| A | TYR51 |
| A | ARG53 |
| site_id | AC9 |
| Number of Residues | 5 |
| Details | binding site for residue HTO A 209 |
| Chain | Residue |
| A | LYS43 |
| A | SER95 |
| A | ASP96 |
| A | SO4206 |
| C | TYR156 |
| site_id | AD1 |
| Number of Residues | 9 |
| Details | binding site for residue HXJ B 201 |
| Chain | Residue |
| A | VAL29 |
| A | ARG31 |
| A | SER166 |
| A | SER167 |
| A | GLY168 |
| B | THR56 |
| B | ASN78 |
| B | ARG79 |
| B | HOH301 |
| site_id | AD2 |
| Number of Residues | 8 |
| Details | binding site for residue HXJ B 202 |
| Chain | Residue |
| B | SER54 |
| B | THR84 |
| B | GLY85 |
| B | TYR108 |
| B | TYR113 |
| B | TYR133 |
| B | TYR137 |
| B | SO4205 |
| site_id | AD3 |
| Number of Residues | 8 |
| Details | binding site for residue HXJ B 203 |
| Chain | Residue |
| B | ASN111 |
| B | TRP112 |
| B | TYR113 |
| B | TRP116 |
| B | TYR137 |
| B | PRO142 |
| B | SO4207 |
| B | HOH303 |
| site_id | AD4 |
| Number of Residues | 3 |
| Details | binding site for residue SO4 B 204 |
| Chain | Residue |
| B | ARG120 |
| B | TYR122 |
| B | LYS123 |
| site_id | AD5 |
| Number of Residues | 5 |
| Details | binding site for residue SO4 B 205 |
| Chain | Residue |
| B | ARG53 |
| B | GLN130 |
| B | TYR133 |
| B | TYR138 |
| B | HXJ202 |
| site_id | AD6 |
| Number of Residues | 4 |
| Details | binding site for residue SO4 B 206 |
| Chain | Residue |
| B | ARG161 |
| B | GLU173 |
| B | HIS175 |
| C | HIS63 |
| site_id | AD7 |
| Number of Residues | 5 |
| Details | binding site for residue SO4 B 207 |
| Chain | Residue |
| B | SER114 |
| B | TRP116 |
| B | ARG144 |
| B | HXJ203 |
| B | HOH303 |
| site_id | AD8 |
| Number of Residues | 4 |
| Details | binding site for residue SO4 B 208 |
| Chain | Residue |
| B | TRP149 |
| B | HIS150 |
| B | SER151 |
| C | ARG127 |
| site_id | AD9 |
| Number of Residues | 7 |
| Details | binding site for residue HXJ C 201 |
| Chain | Residue |
| B | ARG31 |
| B | SER166 |
| B | SER167 |
| B | GLY168 |
| C | THR56 |
| C | ASN78 |
| C | ARG79 |
| site_id | AE1 |
| Number of Residues | 9 |
| Details | binding site for residue HXJ C 202 |
| Chain | Residue |
| C | TRP112 |
| C | TYR113 |
| C | TYR133 |
| C | TYR137 |
| C | SO4206 |
| C | SER54 |
| C | THR84 |
| C | GLY85 |
| C | TYR108 |
| site_id | AE2 |
| Number of Residues | 7 |
| Details | binding site for residue HXJ C 203 |
| Chain | Residue |
| C | ASN111 |
| C | TRP112 |
| C | TYR113 |
| C | TRP116 |
| C | TYR137 |
| C | PRO142 |
| C | SO4208 |
| site_id | AE3 |
| Number of Residues | 10 |
| Details | binding site for residue HXJ C 204 |
| Chain | Residue |
| C | LEU26 |
| C | ARG31 |
| C | TYR110 |
| C | SER166 |
| C | SER167 |
| C | GLY168 |
| D | THR56 |
| D | ASN78 |
| D | ARG79 |
| D | VAL82 |
| site_id | AE4 |
| Number of Residues | 4 |
| Details | binding site for residue SO4 C 205 |
| Chain | Residue |
| C | ARG120 |
| C | VAL121 |
| C | TYR122 |
| C | LYS123 |
| site_id | AE5 |
| Number of Residues | 5 |
| Details | binding site for residue SO4 C 206 |
| Chain | Residue |
| C | ARG53 |
| C | GLN130 |
| C | TYR133 |
| C | TYR138 |
| C | HXJ202 |
| site_id | AE6 |
| Number of Residues | 5 |
| Details | binding site for residue SO4 C 207 |
| Chain | Residue |
| C | ARG161 |
| C | GLU173 |
| C | HIS175 |
| C | HOH307 |
| D | HIS63 |
| site_id | AE7 |
| Number of Residues | 3 |
| Details | binding site for residue SO4 C 208 |
| Chain | Residue |
| C | SER114 |
| C | ARG144 |
| C | HXJ203 |
| site_id | AE8 |
| Number of Residues | 11 |
| Details | binding site for residue HXJ D 201 |
| Chain | Residue |
| D | SER54 |
| D | ALA83 |
| D | THR84 |
| D | GLY85 |
| D | TYR108 |
| D | TRP112 |
| D | TYR113 |
| D | TYR133 |
| D | TYR137 |
| D | SO4205 |
| D | HOH303 |
| site_id | AE9 |
| Number of Residues | 7 |
| Details | binding site for residue HXJ D 202 |
| Chain | Residue |
| D | ASN111 |
| D | TRP112 |
| D | TYR113 |
| D | TRP116 |
| D | TYR137 |
| D | PRO142 |
| D | SO4207 |
| site_id | AF1 |
| Number of Residues | 7 |
| Details | binding site for residue HXJ D 203 |
| Chain | Residue |
| A | ASN78 |
| A | ARG79 |
| D | ARG31 |
| D | TYR110 |
| D | SER166 |
| D | SER167 |
| D | GLY168 |
| site_id | AF2 |
| Number of Residues | 3 |
| Details | binding site for residue SO4 D 204 |
| Chain | Residue |
| D | ARG120 |
| D | TYR122 |
| D | LYS123 |
| site_id | AF3 |
| Number of Residues | 5 |
| Details | binding site for residue SO4 D 205 |
| Chain | Residue |
| D | ARG53 |
| D | GLN130 |
| D | TYR133 |
| D | TYR138 |
| D | HXJ201 |
| site_id | AF4 |
| Number of Residues | 4 |
| Details | binding site for residue SO4 D 206 |
| Chain | Residue |
| A | HIS63 |
| D | ARG161 |
| D | GLU173 |
| D | HIS175 |
| site_id | AF5 |
| Number of Residues | 4 |
| Details | binding site for residue SO4 D 207 |
| Chain | Residue |
| D | SER114 |
| D | TRP116 |
| D | ARG144 |
| D | HXJ202 |
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 |
