4DOJ
Crystal structure of BetP in outward-facing conformation
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0005886 | cellular_component | plasma membrane |
| A | 0015293 | molecular_function | symporter activity |
| A | 0016020 | cellular_component | membrane |
| A | 0022857 | molecular_function | transmembrane transporter activity |
| A | 0042802 | molecular_function | identical protein binding |
| A | 0046872 | molecular_function | metal ion binding |
| A | 0055085 | biological_process | transmembrane transport |
| A | 0071705 | biological_process | nitrogen compound transport |
| B | 0005886 | cellular_component | plasma membrane |
| B | 0015293 | molecular_function | symporter activity |
| B | 0016020 | cellular_component | membrane |
| B | 0022857 | molecular_function | transmembrane transporter activity |
| B | 0042802 | molecular_function | identical protein binding |
| B | 0046872 | molecular_function | metal ion binding |
| B | 0055085 | biological_process | transmembrane transport |
| B | 0071705 | biological_process | nitrogen compound transport |
| C | 0005886 | cellular_component | plasma membrane |
| C | 0015293 | molecular_function | symporter activity |
| C | 0016020 | cellular_component | membrane |
| C | 0022857 | molecular_function | transmembrane transporter activity |
| C | 0042802 | molecular_function | identical protein binding |
| C | 0046872 | molecular_function | metal ion binding |
| C | 0055085 | biological_process | transmembrane transport |
| C | 0071705 | biological_process | nitrogen compound transport |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE CL A 601 |
| Chain | Residue |
| A | ASN177 |
| A | GLY179 |
| B | SER354 |
| site_id | AC2 |
| Number of Residues | 11 |
| Details | BINDING SITE FOR RESIDUE PGT A 602 |
| Chain | Residue |
| A | TYR550 |
| A | TYR553 |
| A | GLN557 |
| C | ARG395 |
| C | LEU399 |
| A | PHE112 |
| A | VAL115 |
| A | ALA119 |
| A | SER120 |
| A | LYS121 |
| A | LEU341 |
| site_id | AC3 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE CHT C 601 |
| Chain | Residue |
| C | ALA148 |
| C | MET150 |
| C | ASP153 |
| C | TRP377 |
| C | PHE380 |
| site_id | AC4 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE CL C 602 |
| Chain | Residue |
| C | ARG126 |
| C | ARG210 |
| C | ILE549 |
Functional Information from PROSITE/UniProt
| site_id | PS01303 |
| Number of Residues | 10 |
| Details | BCCT BCCT family of transporters signature. SWTIfYWaWW |
| Chain | Residue | Details |
| A | SER365-TRP374 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 738 |
| Details | TRANSMEM: Helical => ECO:0000269|PubMed:24141878 |
| Chain | Residue | Details |
| A | TRP60-PHE80 | |
| A | ILE452-MET476 | |
| A | TRP490-GLY510 | |
| A | VAL521-VAL541 | |
| B | TRP60-PHE80 | |
| B | LEU99-ALA119 | |
| B | THR138-GLY158 | |
| B | MET186-TYR206 | |
| B | LEU237-GLY257 | |
| B | TRP277-SER296 | |
| B | LYS300-VAL323 | |
| A | LEU99-ALA119 | |
| B | TRP366-ALA386 | |
| B | PHE397-GLY417 | |
| B | ILE452-MET476 | |
| B | TRP490-GLY510 | |
| B | VAL521-VAL541 | |
| C | TRP60-PHE80 | |
| C | LEU99-ALA119 | |
| C | THR138-GLY158 | |
| C | MET186-TYR206 | |
| C | LEU237-GLY257 | |
| A | THR138-GLY158 | |
| C | TRP277-SER296 | |
| C | LYS300-VAL323 | |
| C | TRP366-ALA386 | |
| C | PHE397-GLY417 | |
| C | ILE452-MET476 | |
| C | TRP490-GLY510 | |
| C | VAL521-VAL541 | |
| A | MET186-TYR206 | |
| A | LEU237-GLY257 | |
| A | TRP277-SER296 | |
| A | LYS300-VAL323 | |
| A | TRP366-ALA386 | |
| A | PHE397-GLY417 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 432 |
| Details | TOPO_DOM: Periplasmic => ECO:0000305 |
| Chain | Residue | Details |
| A | LYS81-ASN98 | |
| B | GLY324-SER365 | |
| B | GLY418-GLN451 | |
| B | GLY511-ASN520 | |
| C | LYS81-ASN98 | |
| C | THR159-THR185 | |
| C | ALA258-ASP276 | |
| C | GLY324-SER365 | |
| C | GLY418-GLN451 | |
| C | GLY511-ASN520 | |
| A | THR159-THR185 | |
| A | ALA258-ASP276 | |
| A | GLY324-SER365 | |
| A | GLY418-GLN451 | |
| A | GLY511-ASN520 | |
| B | LYS81-ASN98 | |
| B | THR159-THR185 | |
| B | ALA258-ASP276 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 207 |
| Details | TOPO_DOM: Cytoplasmic => ECO:0000305 |
| Chain | Residue | Details |
| A | SER120-ARG137 | |
| B | GLY477-LYS489 | |
| C | SER120-ARG137 | |
| C | SER207-LYS236 | |
| C | GLY297-GLY299 | |
| C | ARG387-GLU396 | |
| C | GLY477-LYS489 | |
| A | SER207-LYS236 | |
| A | GLY297-GLY299 | |
| A | ARG387-GLU396 | |
| A | GLY477-LYS489 | |
| B | SER120-ARG137 | |
| B | SER207-LYS236 | |
| B | GLY297-GLY299 | |
| B | ARG387-GLU396 |
| site_id | SWS_FT_FI4 |
| Number of Residues | 159 |
| Details | TOPO_DOM: Cytoplasmic => ECO:0000305|PubMed:9446558 |
| Chain | Residue | Details |
| A | LYS542-ARG595 | |
| B | LYS542-ARG595 | |
| C | LYS542-ARG595 |
| site_id | SWS_FT_FI5 |
| Number of Residues | 6 |
| Details | BINDING: BINDING => ECO:0000305|PubMed:19262666, ECO:0000305|PubMed:22940865, ECO:0000305|PubMed:25023443 |
| Chain | Residue | Details |
| A | ALA147 | |
| A | MET150 | |
| B | ALA147 | |
| B | MET150 | |
| C | ALA147 | |
| C | MET150 |
| site_id | SWS_FT_FI6 |
| Number of Residues | 9 |
| Details | BINDING: BINDING => ECO:0000305|PubMed:19262666 |
| Chain | Residue | Details |
| A | ALA148 | |
| A | SER306 | |
| A | MET310 | |
| B | ALA148 | |
| B | SER306 | |
| B | MET310 | |
| C | ALA148 | |
| C | SER306 | |
| C | MET310 |
| site_id | SWS_FT_FI7 |
| Number of Residues | 6 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:22940865, ECO:0007744|PDB:4AIN |
| Chain | Residue | Details |
| A | ILE152 | |
| A | SER253 | |
| B | ILE152 | |
| B | SER253 | |
| C | ILE152 | |
| C | SER253 |
| site_id | SWS_FT_FI8 |
| Number of Residues | 3 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:19262666, ECO:0000269|PubMed:22940865, ECO:0007744|PDB:4AIN |
| Chain | Residue | Details |
| A | TRP373 | |
| B | TRP373 | |
| C | TRP373 |
