2YVX
Crystal structure of magnesium transporter MgtE
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0000287 | molecular_function | magnesium ion binding |
| A | 0005886 | cellular_component | plasma membrane |
| A | 0006812 | biological_process | monoatomic cation transport |
| A | 0008324 | molecular_function | monoatomic cation transmembrane transporter activity |
| A | 0015095 | molecular_function | magnesium ion transmembrane transporter activity |
| A | 0015693 | biological_process | magnesium ion transport |
| A | 0016020 | cellular_component | membrane |
| A | 0042802 | molecular_function | identical protein binding |
| A | 0042803 | molecular_function | protein homodimerization activity |
| A | 0046872 | molecular_function | metal ion binding |
| A | 0098655 | biological_process | monoatomic cation transmembrane transport |
| A | 1903830 | biological_process | magnesium ion transmembrane transport |
| B | 0000287 | molecular_function | magnesium ion binding |
| B | 0005886 | cellular_component | plasma membrane |
| B | 0006812 | biological_process | monoatomic cation transport |
| B | 0008324 | molecular_function | monoatomic cation transmembrane transporter activity |
| B | 0015095 | molecular_function | magnesium ion transmembrane transporter activity |
| B | 0015693 | biological_process | magnesium ion transport |
| B | 0016020 | cellular_component | membrane |
| B | 0042802 | molecular_function | identical protein binding |
| B | 0042803 | molecular_function | protein homodimerization activity |
| B | 0046872 | molecular_function | metal ion binding |
| B | 0098655 | biological_process | monoatomic cation transmembrane transport |
| B | 1903830 | biological_process | magnesium ion transmembrane transport |
| C | 0000287 | molecular_function | magnesium ion binding |
| C | 0005886 | cellular_component | plasma membrane |
| C | 0006812 | biological_process | monoatomic cation transport |
| C | 0008324 | molecular_function | monoatomic cation transmembrane transporter activity |
| C | 0015095 | molecular_function | magnesium ion transmembrane transporter activity |
| C | 0015693 | biological_process | magnesium ion transport |
| C | 0016020 | cellular_component | membrane |
| C | 0042802 | molecular_function | identical protein binding |
| C | 0042803 | molecular_function | protein homodimerization activity |
| C | 0046872 | molecular_function | metal ion binding |
| C | 0098655 | biological_process | monoatomic cation transmembrane transport |
| C | 1903830 | biological_process | magnesium ion transmembrane transport |
| D | 0000287 | molecular_function | magnesium ion binding |
| D | 0005886 | cellular_component | plasma membrane |
| D | 0006812 | biological_process | monoatomic cation transport |
| D | 0008324 | molecular_function | monoatomic cation transmembrane transporter activity |
| D | 0015095 | molecular_function | magnesium ion transmembrane transporter activity |
| D | 0015693 | biological_process | magnesium ion transport |
| D | 0016020 | cellular_component | membrane |
| D | 0042802 | molecular_function | identical protein binding |
| D | 0042803 | molecular_function | protein homodimerization activity |
| D | 0046872 | molecular_function | metal ion binding |
| D | 0098655 | biological_process | monoatomic cation transmembrane transport |
| D | 1903830 | biological_process | magnesium ion transmembrane transport |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 1 |
| Details | BINDING SITE FOR RESIDUE MG B 451 |
| Chain | Residue |
| B | ASP432 |
| site_id | AC2 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE MG C 451 |
| Chain | Residue |
| C | ALA428 |
| C | ASP432 |
| site_id | AC3 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE MG A 451 |
| Chain | Residue |
| A | GLU216 |
| A | GLU258 |
| A | ASP259 |
| A | ASP418 |
| site_id | AC4 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE MG B 452 |
| Chain | Residue |
| B | GLU258 |
| B | ASP259 |
| B | ASP418 |
| B | GLU216 |
| B | GLU255 |
| site_id | AC5 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE MG C 452 |
| Chain | Residue |
| C | GLU216 |
| C | ASP259 |
| C | ASP418 |
| site_id | AC6 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE MG D 451 |
| Chain | Residue |
| D | ASP259 |
| D | ASP418 |
| site_id | AC7 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE MG A 452 |
| Chain | Residue |
| A | ASP91 |
| A | ASP92 |
| A | GLU166 |
| A | ASP247 |
| site_id | AC8 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE MG A 453 |
| Chain | Residue |
| A | ALA223 |
| A | ASP226 |
| site_id | AC9 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE MG B 453 |
| Chain | Residue |
| B | ASP91 |
| B | GLU166 |
| B | THR244 |
| B | ASP247 |
| site_id | BC1 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE MG B 454 |
| Chain | Residue |
| A | ASP246 |
| A | ASP250 |
| B | ALA223 |
| B | ASP226 |
| site_id | BC2 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE MG C 453 |
| Chain | Residue |
| C | ASP92 |
| C | ASP247 |
| site_id | BC3 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE MG D 452 |
| Chain | Residue |
| D | GLU166 |
| D | THR244 |
| D | ASP246 |
| D | ASP247 |
| site_id | BC4 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE MG D 453 |
| Chain | Residue |
| C | ASP246 |
| C | ASP250 |
| D | ALA223 |
| D | ASP226 |
| site_id | BC5 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE MG C 454 |
| Chain | Residue |
| C | ALA223 |
| C | ASP226 |
| D | ASP246 |
| D | ASP250 |
| site_id | BC6 |
| Number of Residues | 1 |
| Details | BINDING SITE FOR RESIDUE MG A 454 |
| Chain | Residue |
| A | GLU255 |
| site_id | BC7 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE MG B 455 |
| Chain | Residue |
| B | ASP214 |
| B | GLU255 |
| site_id | BC8 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE MG C 455 |
| Chain | Residue |
| C | ASP214 |
| C | GLU216 |
| C | GLU255 |
| site_id | BC9 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE MG D 454 |
| Chain | Residue |
| D | GLU255 |
| D | GLU258 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 1220 |
| Details | TOPO_DOM: Cytoplasmic => ECO:0000269|PubMed:17700703, ECO:0000269|PubMed:25367295 |
| Chain | Residue | Details |
| A | MET1-LEU283 | |
| D | MET1-LEU283 | |
| D | ILE338-ASP351 | |
| D | PHE410-ALA420 | |
| A | ILE338-ASP351 | |
| A | PHE410-ALA420 | |
| B | MET1-LEU283 | |
| B | ILE338-ASP351 | |
| B | PHE410-ALA420 | |
| C | MET1-LEU283 | |
| C | ILE338-ASP351 | |
| C | PHE410-ALA420 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 468 |
| Details | TRANSMEM: Helical => ECO:0000269|PubMed:25367295, ECO:0007744|PDB:4U9L, ECO:0007744|PDB:4U9N, ECO:0007744|PDB:4WIB |
| Chain | Residue | Details |
| A | ALA284-PHE306 | |
| B | LEU421-ALA443 | |
| C | ALA284-PHE306 | |
| C | LEU316-LEU337 | |
| C | TRP352-ASP381 | |
| C | LEU386-PRO409 | |
| C | LEU421-ALA443 | |
| D | ALA284-PHE306 | |
| D | LEU316-LEU337 | |
| D | TRP352-ASP381 | |
| D | LEU386-PRO409 | |
| A | LEU316-LEU337 | |
| D | LEU421-ALA443 | |
| A | TRP352-ASP381 | |
| A | LEU386-PRO409 | |
| A | LEU421-ALA443 | |
| B | ALA284-PHE306 | |
| B | LEU316-LEU337 | |
| B | TRP352-ASP381 | |
| B | LEU386-PRO409 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 68 |
| Details | TOPO_DOM: Periplasmic => ECO:0000269|PubMed:17700703, ECO:0000269|PubMed:25367295 |
| Chain | Residue | Details |
| A | GLU307-ALA315 | |
| D | GLU307-ALA315 | |
| D | GLY382-LEU385 | |
| D | ARG444-VAL450 | |
| A | GLY382-LEU385 | |
| A | ARG444-VAL450 | |
| B | GLU307-ALA315 | |
| B | GLY382-LEU385 | |
| B | ARG444-VAL450 | |
| C | GLU307-ALA315 | |
| C | GLY382-LEU385 | |
| C | ARG444-VAL450 |
| site_id | SWS_FT_FI4 |
| Number of Residues | 20 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:19798051, ECO:0000269|PubMed:28747715 |
| Chain | Residue | Details |
| A | GLU59 | |
| B | ASP432 | |
| C | GLU59 | |
| C | GLU216 | |
| C | GLU255 | |
| C | GLU258 | |
| C | ASP432 | |
| D | GLU59 | |
| D | GLU216 | |
| D | GLU255 | |
| D | GLU258 | |
| A | GLU216 | |
| D | ASP432 | |
| A | GLU255 | |
| A | GLU258 | |
| A | ASP432 | |
| B | GLU59 | |
| B | GLU216 | |
| B | GLU255 | |
| B | GLU258 |
| site_id | SWS_FT_FI5 |
| Number of Residues | 16 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:19798051, ECO:0000269|PubMed:28747715, ECO:0007744|PDB:2ZY9, ECO:0007744|PDB:5X9G, ECO:0007744|PDB:5X9H |
| Chain | Residue | Details |
| A | ASP91 | |
| C | ASP95 | |
| C | GLY136 | |
| C | ASP247 | |
| D | ASP91 | |
| D | ASP95 | |
| D | GLY136 | |
| D | ASP247 | |
| A | ASP95 | |
| A | GLY136 | |
| A | ASP247 | |
| B | ASP91 | |
| B | ASP95 | |
| B | GLY136 | |
| B | ASP247 | |
| C | ASP91 |
| site_id | SWS_FT_FI6 |
| Number of Residues | 20 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:28747715, ECO:0007744|PDB:5X9G, ECO:0007744|PDB:5X9H |
| Chain | Residue | Details |
| A | TYR170 | |
| B | VAL207 | |
| C | TYR170 | |
| C | SER185 | |
| C | ARG187 | |
| C | ASP188 | |
| C | VAL207 | |
| D | TYR170 | |
| D | SER185 | |
| D | ARG187 | |
| D | ASP188 | |
| A | SER185 | |
| D | VAL207 | |
| A | ARG187 | |
| A | ASP188 | |
| A | VAL207 | |
| B | TYR170 | |
| B | SER185 | |
| B | ARG187 | |
| B | ASP188 |
| site_id | SWS_FT_FI7 |
| Number of Residues | 12 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:19798051, ECO:0000269|PubMed:28747715, ECO:0007744|PDB:2ZY9, ECO:0007744|PDB:5X9H |
| Chain | Residue | Details |
| A | ALA223 | |
| D | ALA223 | |
| D | ASP226 | |
| D | ASP250 | |
| A | ASP226 | |
| A | ASP250 | |
| B | ALA223 | |
| B | ASP226 | |
| B | ASP250 | |
| C | ALA223 | |
| C | ASP226 | |
| C | ASP250 |
| site_id | SWS_FT_FI8 |
| Number of Residues | 8 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:19798051, ECO:0000269|PubMed:28747715, ECO:0007744|PDB:2ZY9 |
| Chain | Residue | Details |
| A | ASP259 | |
| A | ASP418 | |
| B | ASP259 | |
| B | ASP418 | |
| C | ASP259 | |
| C | ASP418 | |
| D | ASP259 | |
| D | ASP418 |
| site_id | SWS_FT_FI9 |
| Number of Residues | 20 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:25367295, ECO:0007744|PDB:4U9N |
| Chain | Residue | Details |
| A | GLU275 | |
| B | HIS383 | |
| C | GLU275 | |
| C | GLN304 | |
| C | GLU307 | |
| C | GLU311 | |
| C | HIS383 | |
| D | GLU275 | |
| D | GLN304 | |
| D | GLU307 | |
| D | GLU311 | |
| A | GLN304 | |
| D | HIS383 | |
| A | GLU307 | |
| A | GLU311 | |
| A | HIS383 | |
| B | GLU275 | |
| B | GLN304 | |
| B | GLU307 | |
| B | GLU311 |
| site_id | SWS_FT_FI10 |
| Number of Residues | 4 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:19798051 |
| Chain | Residue | Details |
| A | ALA428 | |
| B | ALA428 | |
| C | ALA428 | |
| D | ALA428 |
