8GHT
Cryo-electron microscopy structure of the zinc transporter from Bordetella bronchiseptica
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0000329 | cellular_component | fungal-type vacuole membrane |
| A | 0005385 | molecular_function | zinc ion transmembrane transporter activity |
| A | 0005886 | cellular_component | plasma membrane |
| A | 0006829 | biological_process | zinc ion transport |
| A | 0016020 | cellular_component | membrane |
| A | 0030001 | biological_process | metal ion transport |
| A | 0046873 | molecular_function | metal ion transmembrane transporter activity |
| A | 0055085 | biological_process | transmembrane transport |
| A | 0071577 | biological_process | zinc ion transmembrane transport |
| B | 0000329 | cellular_component | fungal-type vacuole membrane |
| B | 0005385 | molecular_function | zinc ion transmembrane transporter activity |
| B | 0005886 | cellular_component | plasma membrane |
| B | 0006829 | biological_process | zinc ion transport |
| B | 0016020 | cellular_component | membrane |
| B | 0030001 | biological_process | metal ion transport |
| B | 0046873 | molecular_function | metal ion transmembrane transporter activity |
| B | 0055085 | biological_process | transmembrane transport |
| B | 0071577 | biological_process | zinc ion transmembrane transport |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 42 |
| Details | TOPO_DOM: Periplasmic => ECO:0000269|PubMed:35857505 |
| Chain | Residue | Details |
| A | MET1-HIS22 | |
| B | MET1-HIS22 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 54 |
| Details | TRANSMEM: Helical => ECO:0000269|PubMed:35857505 |
| Chain | Residue | Details |
| A | PRO23-GLY50 | |
| B | PRO23-GLY50 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 8 |
| Details | TOPO_DOM: Extracellular => ECO:0000269|PubMed:35857505 |
| Chain | Residue | Details |
| A | GLU51-HIS55 | |
| B | GLU51-HIS55 |
| site_id | SWS_FT_FI4 |
| Number of Residues | 402 |
| Details | TRANSMEM: Helical => ECO:0000269|PubMed:28875161 |
| Chain | Residue | Details |
| A | VAL56-ARG81 | |
| A | SER84-VAL119 | |
| A | GLY122-TYR145 | |
| A | ARG166-ALA190 | |
| A | ASP193-VAL222 | |
| A | PRO225-SER251 | |
| A | LEU256-HIS275 | |
| A | THR288-LEU308 | |
| B | VAL56-ARG81 | |
| B | SER84-VAL119 | |
| B | GLY122-TYR145 | |
| B | ARG166-ALA190 | |
| B | ASP193-VAL222 | |
| B | PRO225-SER251 | |
| B | LEU256-HIS275 | |
| B | THR288-LEU308 |
| site_id | SWS_FT_FI5 |
| Number of Residues | 64 |
| Details | TOPO_DOM: Periplasmic => ECO:0000305|PubMed:28875161 |
| Chain | Residue | Details |
| A | ALA82-ILE83 | |
| A | PHE146-ASN165 | |
| A | GLY223-LEU224 | |
| A | GLU276-GLU287 | |
| B | ALA82-ILE83 | |
| B | PHE146-ASN165 | |
| B | GLY223-LEU224 | |
| B | GLU276-GLU287 |
| site_id | SWS_FT_FI6 |
| Number of Residues | 12 |
| Details | TOPO_DOM: Extracellular => ECO:0000305|PubMed:28875161 |
| Chain | Residue | Details |
| A | GLY120-PRO121 | |
| A | THR191-GLY192 | |
| A | SER252-ALA255 | |
| A | GLY309 | |
| B | GLY120-PRO121 | |
| B | THR191-GLY192 | |
| B | SER252-ALA255 | |
| B | GLY309 |
| site_id | SWS_FT_FI7 |
| Number of Residues | 4 |
| Details | BINDING: M7 metal binding site => ECO:0000269|PubMed:28875161, ECO:0007744|PDB:5TSA |
| Chain | Residue | Details |
| A | ASP89 | |
| A | HIS286 | |
| B | ASP89 | |
| B | HIS286 |
| site_id | SWS_FT_FI8 |
| Number of Residues | 2 |
| Details | BINDING: M1 metal binding site => ECO:0000269|PubMed:28875161, ECO:0000269|PubMed:31914589, ECO:0000269|PubMed:35857505, ECO:0007744|PDB:5TSB, ECO:0007744|PDB:6PGI, ECO:0007744|PDB:7Z6M |
| Chain | Residue | Details |
| A | MET99 | |
| B | MET99 |
| site_id | SWS_FT_FI9 |
| Number of Residues | 2 |
| Details | BINDING: M6 metal binding site => ECO:0000269|PubMed:28875161, ECO:0007744|PDB:5TSA |
| Chain | Residue | Details |
| A | ASP144 | |
| B | ASP144 |
| site_id | SWS_FT_FI10 |
| Number of Residues | 4 |
| Details | BINDING: M5 metal binding site => ECO:0000269|PubMed:28875161, ECO:0007744|PDB:5TSA |
| Chain | Residue | Details |
| A | HIS177 | |
| A | GLU276 | |
| B | HIS177 | |
| B | GLU276 |
| site_id | SWS_FT_FI11 |
| Number of Residues | 6 |
| Details | BINDING: M2 metal binding site => ECO:0000269|PubMed:28875161, ECO:0007744|PDB:5TSA, ECO:0007744|PDB:5TSB |
| Chain | Residue | Details |
| A | ASN178 | |
| A | ASP208 | |
| A | GLU240 | |
| B | ASN178 | |
| B | ASP208 | |
| B | GLU240 |
| site_id | SWS_FT_FI12 |
| Number of Residues | 6 |
| Details | BINDING: M1 metal binding site => ECO:0000269|PubMed:28875161, ECO:0007744|PDB:5TSA |
| Chain | Residue | Details |
| A | GLU181 | |
| A | GLN207 | |
| A | GLU211 | |
| B | GLU181 | |
| B | GLN207 | |
| B | GLU211 |
| site_id | SWS_FT_FI13 |
| Number of Residues | 2 |
| Details | BINDING: M3 metal binding site => ECO:0000269|PubMed:28875161, ECO:0007744|PDB:5TSA |
| Chain | Residue | Details |
| A | HIS275 | |
| B | HIS275 |
