Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0016020 | cellular_component | membrane |
| B | 0016020 | cellular_component | membrane |
| C | 0016020 | cellular_component | membrane |
| D | 0016020 | cellular_component | membrane |
| E | 0016020 | cellular_component | membrane |
| F | 0016020 | cellular_component | membrane |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 2 |
| Details | binding site for residue XP4 A 201 |
| Chain | Residue |
| A | XP4203 |
| F | XP4201 |
| site_id | AC2 |
| Number of Residues | 1 |
| Details | binding site for residue XP4 A 202 |
| site_id | AC3 |
| Number of Residues | 7 |
| Details | binding site for residue XP4 A 203 |
| Chain | Residue |
| B | XP4201 |
| A | PHE97 |
| A | XP4201 |
| B | GLY38 |
| B | LEU39 |
| B | THR96 |
| B | PHE97 |
| site_id | AC4 |
| Number of Residues | 2 |
| Details | binding site for residue XP4 B 201 |
| Chain | Residue |
| A | XP4203 |
| B | XP4203 |
| site_id | AC5 |
| Number of Residues | 1 |
| Details | binding site for residue XP4 B 202 |
| site_id | AC6 |
| Number of Residues | 6 |
| Details | binding site for residue XP4 B 203 |
| Chain | Residue |
| B | PHE97 |
| B | XP4201 |
| C | PHE34 |
| C | THR96 |
| C | PHE97 |
| C | XP4201 |
| site_id | AC7 |
| Number of Residues | 2 |
| Details | binding site for residue XP4 C 201 |
| Chain | Residue |
| B | XP4203 |
| C | XP4203 |
| site_id | AC8 |
| Number of Residues | 1 |
| Details | binding site for residue XP4 C 202 |
| site_id | AC9 |
| Number of Residues | 7 |
| Details | binding site for residue XP4 C 203 |
| Chain | Residue |
| C | PHE97 |
| C | XP4201 |
| D | PHE34 |
| D | LEU39 |
| D | THR96 |
| D | PHE97 |
| D | XP4201 |
| site_id | AD1 |
| Number of Residues | 2 |
| Details | binding site for residue XP4 D 201 |
| Chain | Residue |
| C | XP4203 |
| D | XP4203 |
| site_id | AD2 |
| Number of Residues | 1 |
| Details | binding site for residue XP4 D 202 |
| site_id | AD3 |
| Number of Residues | 7 |
| Details | binding site for residue XP4 D 203 |
| Chain | Residue |
| D | PHE97 |
| D | XP4201 |
| E | GLY38 |
| E | LEU39 |
| E | THR96 |
| E | PHE97 |
| E | XP4201 |
| site_id | AD4 |
| Number of Residues | 2 |
| Details | binding site for residue XP4 E 201 |
| Chain | Residue |
| D | XP4203 |
| E | XP4203 |
| site_id | AD5 |
| Number of Residues | 1 |
| Details | binding site for residue XP4 E 202 |
| site_id | AD6 |
| Number of Residues | 6 |
| Details | binding site for residue XP4 E 203 |
| Chain | Residue |
| E | PHE97 |
| E | XP4201 |
| F | PHE34 |
| F | THR96 |
| F | PHE97 |
| F | XP4202 |
| site_id | AD7 |
| Number of Residues | 7 |
| Details | binding site for residue XP4 F 201 |
| Chain | Residue |
| A | PHE34 |
| A | LEU39 |
| A | THR96 |
| A | PHE97 |
| A | XP4201 |
| F | PHE97 |
| F | XP4202 |
| site_id | AD8 |
| Number of Residues | 2 |
| Details | binding site for residue XP4 F 202 |
| Chain | Residue |
| E | XP4203 |
| F | XP4201 |
| site_id | AD9 |
| Number of Residues | 1 |
| Details | binding site for residue XP4 F 203 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 246 |
| Details | TOPO_DOM: Periplasmic => ECO:0000255 |
| Chain | Residue | Details |
| A | MET1 | |
| C | HIS54-VAL55 | |
| C | HIS123-ASP140 | |
| C | GLN192-VAL195 | |
| D | MET1 | |
| D | HIS54-VAL55 | |
| D | HIS123-ASP140 | |
| D | GLN192-VAL195 | |
| E | MET1 | |
| E | HIS54-VAL55 | |
| E | HIS123-ASP140 | |
| A | HIS54-VAL55 | |
| E | GLN192-VAL195 | |
| F | MET1 | |
| F | HIS54-VAL55 | |
| F | HIS123-ASP140 | |
| F | GLN192-VAL195 | |
| A | HIS123-ASP140 | |
| A | GLN192-VAL195 | |
| B | MET1 | |
| B | HIS54-VAL55 | |
| B | HIS123-ASP140 | |
| B | GLN192-VAL195 | |
| C | MET1 | |
| site_id | SWS_FT_FI2 |
| Number of Residues | 660 |
| Details | TRANSMEM: Helical => ECO:0000255 |
| Chain | Residue | Details |
| A | LEU2-LEU21 | |
| B | TYR104-SER122 | |
| B | TRP141-ILE158 | |
| B | TRP172-ILE191 | |
| C | LEU2-LEU21 | |
| C | PHE34-LEU53 | |
| C | PHE75-ILE93 | |
| C | TYR104-SER122 | |
| C | TRP141-ILE158 | |
| C | TRP172-ILE191 | |
| D | LEU2-LEU21 | |
| A | PHE34-LEU53 | |
| D | PHE34-LEU53 | |
| D | PHE75-ILE93 | |
| D | TYR104-SER122 | |
| D | TRP141-ILE158 | |
| D | TRP172-ILE191 | |
| E | LEU2-LEU21 | |
| E | PHE34-LEU53 | |
| E | PHE75-ILE93 | |
| E | TYR104-SER122 | |
| E | TRP141-ILE158 | |
| A | PHE75-ILE93 | |
| E | TRP172-ILE191 | |
| F | LEU2-LEU21 | |
| F | PHE34-LEU53 | |
| F | PHE75-ILE93 | |
| F | TYR104-SER122 | |
| F | TRP141-ILE158 | |
| F | TRP172-ILE191 | |
| A | TYR104-SER122 | |
| A | TRP141-ILE158 | |
| A | TRP172-ILE191 | |
| B | LEU2-LEU21 | |
| B | PHE34-LEU53 | |
| B | PHE75-ILE93 | |
| site_id | SWS_FT_FI3 |
| Number of Residues | 192 |
| Details | TOPO_DOM: Cytoplasmic => ECO:0000255 |
| Chain | Residue | Details |
| A | THR22-ASN33 | |
| D | THR22-ASN33 | |
| D | ASN94-PRO103 | |
| D | GLU159-PRO171 | |
| E | THR22-ASN33 | |
| E | ASN94-PRO103 | |
| E | GLU159-PRO171 | |
| F | THR22-ASN33 | |
| F | ASN94-PRO103 | |
| F | GLU159-PRO171 | |
| A | ASN94-PRO103 | |
| A | GLU159-PRO171 | |
| B | THR22-ASN33 | |
| B | ASN94-PRO103 | |
| B | GLU159-PRO171 | |
| C | THR22-ASN33 | |
| C | ASN94-PRO103 | |
| C | GLU159-PRO171 | |
