4AIN
Crystal structure of BetP with asymmetric protomers.
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 C 1554 |
| Chain | Residue |
| B | GLY179 |
| C | SER354 |
| C | ALA355 |
| site_id | AC2 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE CL C 1555 |
| Chain | Residue |
| A | SER354 |
| A | ALA355 |
| C | ASN177 |
| C | GLY179 |
| site_id | AC3 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE NA B 1558 |
| Chain | Residue |
| B | PHE464 |
| B | THR467 |
| B | SER468 |
| B | ALA147 |
| B | MET150 |
| site_id | AC4 |
| Number of Residues | 9 |
| Details | BINDING SITE FOR RESIDUE BET B 1559 |
| Chain | Residue |
| B | GLY149 |
| B | GLY151 |
| B | ILE152 |
| B | GLY153 |
| B | TYR197 |
| B | SER253 |
| B | TRP373 |
| B | TRP374 |
| B | TRP377 |
| site_id | AC5 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE PEG B 1560 |
| Chain | Residue |
| B | ASN168 |
| B | GLU175 |
| C | GLU132 |
| site_id | AC6 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE BET C 1556 |
| Chain | Residue |
| C | ALA148 |
| C | MET150 |
| C | GLY151 |
| C | TRP377 |
| C | PHE380 |
| C | HOH2006 |
| site_id | AC7 |
| Number of Residues | 1 |
| Details | BINDING SITE FOR RESIDUE CL B 1561 |
| Chain | Residue |
| A | GLY179 |
| site_id | AC8 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE CL C 1557 |
| Chain | Residue |
| C | ARG126 |
| C | ASP131 |
| C | ARG210 |
| C | ILE549 |
| site_id | AC9 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE FLC C 1558 |
| Chain | Residue |
| C | VAL322 |
| C | GLY324 |
| C | THR326 |
| site_id | BC1 |
| Number of Residues | 1 |
| Details | BINDING SITE FOR RESIDUE CM5 C 1559 |
| Chain | Residue |
| C | LYS81 |
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 | 718 |
| Details | Transmembrane: {"description":"Helical","evidences":[{"source":"PubMed","id":"24141878","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 405 |
| Details | Topological domain: {"description":"Periplasmic","evidences":[{"evidenceCode":"ECO:0000305"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 188 |
| 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 |
