4C7R
Inward facing conformation of the trimeric betaine transporter BetP in complex with lipids
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 | 5 |
| Details | BINDING SITE FOR RESIDUE FLC A 1001 |
| Chain | Residue |
| A | ALA148 |
| A | GLY149 |
| A | GLY151 |
| A | TRP377 |
| A | PHE380 |
| site_id | AC2 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE FLC B 1001 |
| Chain | Residue |
| B | TRP377 |
| B | ALA147 |
| B | ALA148 |
| B | GLY149 |
| B | MET150 |
| site_id | AC3 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE FLC C 1001 |
| Chain | Residue |
| C | ALA148 |
| C | MET150 |
| C | TRP377 |
| C | PHE380 |
| C | HOH2006 |
| C | HOH2014 |
| C | HOH2020 |
| site_id | AC4 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE CL C 1562 |
| Chain | Residue |
| C | ARG126 |
| C | ASP131 |
| C | ARG210 |
| C | ILE549 |
| site_id | AC5 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE CL B 1553 |
| Chain | Residue |
| B | ARG126 |
| B | ARG210 |
| site_id | AC6 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE CL A 1587 |
| Chain | Residue |
| A | ASN177 |
| A | GLY179 |
| B | ALA355 |
| site_id | AC7 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE CL C 1563 |
| Chain | Residue |
| B | GLY179 |
| C | ALA355 |
| site_id | AC8 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE CL C 1564 |
| Chain | Residue |
| A | ALA355 |
| C | ASN177 |
| C | GLY179 |
| site_id | AC9 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE PGT A 1588 |
| Chain | Residue |
| A | ALA119 |
| A | LEU399 |
| A | PGT1589 |
| A | PGT1591 |
| A | PGT1592 |
| B | SER120 |
| B | LYS121 |
| B | PGT1554 |
| site_id | BC1 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE PGT B 1554 |
| Chain | Residue |
| A | PGT1588 |
| A | PGT1592 |
| B | PHE112 |
| B | PHE113 |
| B | ALA119 |
| B | VAL541 |
| B | TYR550 |
| site_id | BC2 |
| Number of Residues | 13 |
| Details | BINDING SITE FOR RESIDUE PGT A 1589 |
| Chain | Residue |
| A | PHE112 |
| A | SER120 |
| A | LYS121 |
| A | PGT1588 |
| A | PGT1590 |
| A | PGT1591 |
| A | PGT1592 |
| C | SER120 |
| C | LYS121 |
| C | LEU191 |
| C | ARG395 |
| C | LEU399 |
| C | LEU403 |
| site_id | BC3 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE PGT C 1565 |
| Chain | Residue |
| C | SER143 |
| C | MET150 |
| C | MET310 |
| C | VAL311 |
| C | ALA313 |
| C | ALA314 |
| C | ILE318 |
| C | PGT1566 |
| site_id | BC4 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE PGT C 1566 |
| Chain | Residue |
| A | ASN98 |
| C | VAL322 |
| C | VAL323 |
| C | GLY324 |
| C | THR326 |
| C | PGT1565 |
| site_id | BC5 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE PGT A 1590 |
| Chain | Residue |
| A | VAL116 |
| A | ARG554 |
| A | ARG558 |
| A | PGT1589 |
| C | ARG126 |
| C | SER393 |
| C | ARG395 |
| C | GLU396 |
| site_id | BC6 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE PGT A 1591 |
| Chain | Residue |
| A | PHE345 |
| A | PGT1588 |
| A | PGT1589 |
| B | PHE345 |
| C | LEU341 |
| site_id | BC7 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE PGT A 1592 |
| Chain | Residue |
| A | PGT1588 |
| A | PGT1589 |
| B | ALA118 |
| B | ALA119 |
| B | ARG395 |
| B | PGT1554 |
| C | TYR550 |
| site_id | BC8 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE PGT C 1567 |
| Chain | Residue |
| C | PHE538 |
| C | VAL541 |
| C | LYS542 |
| C | CM51568 |
| site_id | BC9 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE CM5 C 1568 |
| Chain | Residue |
| C | ILE238 |
| C | PGT1567 |
| C | ILE225 |
| C | LYS228 |
| site_id | CC1 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE FLC C 1569 |
| Chain | Residue |
| C | ARG167 |
| C | ASN168 |
| C | GLU175 |
| site_id | CC2 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE PEG B 1555 |
| Chain | Residue |
| B | SER306 |
| B | PHE384 |
| B | THR467 |
| B | SER471 |
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 | Transmembrane: {"description":"Helical","evidences":[{"source":"PubMed","id":"24141878","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 432 |
| Details | Topological domain: {"description":"Periplasmic","evidences":[{"evidenceCode":"ECO:0000305"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 207 |
| Details | Topological domain: {"description":"Cytoplasmic","evidences":[{"evidenceCode":"ECO:0000305"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 6 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"19262666","evidenceCode":"ECO:0000305"},{"source":"PubMed","id":"22940865","evidenceCode":"ECO:0000305"},{"source":"PubMed","id":"25023443","evidenceCode":"ECO:0000305"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI5 |
| Number of Residues | 9 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"19262666","evidenceCode":"ECO:0000305"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI6 |
| Number of Residues | 6 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"22940865","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"4AIN","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI7 |
| Number of Residues | 12 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"19262666","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"22940865","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"4AIN","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |






