4WDC
High-resolution crystal structure of water-soluble FraC (mutation F16P)
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 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 2 |
| Details | BINDING: in subunit A; in oligomeric forms only => ECO:0000305|PubMed:25716479 |
| Chain | Residue | Details |
| A | ARG31 | |
| A | GLY168 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 3 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:28630155 |
| Chain | Residue | Details |
| A | TYR51 | |
| A | ARG53 | |
| A | TYR138 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 9 |
| Details | BINDING: in monomeric and oligomeric forms => ECO:0000305|PubMed:25716479 |
| Chain | Residue | Details |
| A | SER54 | |
| A | GLY85 | |
| A | TYR108 | |
| A | TYR113 | |
| A | SER114 | |
| A | TRP116 | |
| A | TYR133 | |
| A | TYR137 | |
| A | ARG144 |
| site_id | SWS_FT_FI4 |
| Number of Residues | 1 |
| Details | BINDING: in subunit B; in oligomeric forms only => ECO:0000305|PubMed:25716479 |
| Chain | Residue | Details |
| A | ARG79 |
| site_id | SWS_FT_FI5 |
| Number of Residues | 1 |
| 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 | PRO16 |
| site_id | SWS_FT_FI6 |
| Number of Residues | 1 |
| 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 |
| site_id | SWS_FT_FI7 |
| Number of Residues | 1 |
| 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 |
| site_id | SWS_FT_FI8 |
| Number of Residues | 1 |
| 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 |
