3OB6
Structure of AdiC(N101A) in the open-to-out Arg+ bound conformation
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0003333 | biological_process | amino acid transmembrane transport |
| A | 0005886 | cellular_component | plasma membrane |
| A | 0006865 | biological_process | amino acid transport |
| A | 0015297 | molecular_function | antiporter activity |
| A | 0015695 | biological_process | organic cation transport |
| A | 0016020 | cellular_component | membrane |
| A | 0022857 | molecular_function | transmembrane transporter activity |
| A | 0043862 | molecular_function | arginine:agmatine antiporter activity |
| A | 0055085 | biological_process | transmembrane transport |
| A | 1905039 | biological_process | carboxylic acid transmembrane transport |
| A | 1990451 | biological_process | cellular stress response to acidic pH |
| B | 0003333 | biological_process | amino acid transmembrane transport |
| B | 0005886 | cellular_component | plasma membrane |
| B | 0006865 | biological_process | amino acid transport |
| B | 0015297 | molecular_function | antiporter activity |
| B | 0015695 | biological_process | organic cation transport |
| B | 0016020 | cellular_component | membrane |
| B | 0022857 | molecular_function | transmembrane transporter activity |
| B | 0043862 | molecular_function | arginine:agmatine antiporter activity |
| B | 0055085 | biological_process | transmembrane transport |
| B | 1905039 | biological_process | carboxylic acid transmembrane transport |
| B | 1990451 | biological_process | cellular stress response to acidic pH |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 9 |
| Details | BINDING SITE FOR RESIDUE ARG A 450 |
| Chain | Residue |
| A | ILE23 |
| A | SER26 |
| A | GLY27 |
| A | ALA96 |
| A | GLY100 |
| A | TRP202 |
| A | ILE205 |
| A | TRP293 |
| A | SER357 |
| site_id | AC2 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE ARG B 450 |
| Chain | Residue |
| B | ASN22 |
| B | ILE23 |
| B | MET24 |
| B | SER26 |
| B | MET104 |
| B | ILE107 |
| B | ILE205 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 168 |
| Details | TOPO_DOM: Cytoplasmic => ECO:0000255 |
| Chain | Residue | Details |
| A | MET1-GLY11 | |
| B | ILE205-ARG222 | |
| B | LYS302-VAL324 | |
| B | ALA371-ARG384 | |
| A | MET63-PRO83 | |
| A | GLY143-LYS145 | |
| A | ILE205-ARG222 | |
| A | LYS302-VAL324 | |
| A | ALA371-ARG384 | |
| B | MET1-GLY11 | |
| B | MET63-PRO83 | |
| B | GLY143-LYS145 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 500 |
| Details | TRANSMEM: Helical => ECO:0007744|PDB:5J4I |
| Chain | Residue | Details |
| A | LEU12-MET24 | |
| A | THR347-ALA370 | |
| A | PRO385-GLY404 | |
| A | GLU409-ASN427 | |
| B | LEU12-MET24 | |
| B | ILE41-LYS62 | |
| B | PHE84-SER113 | |
| B | VAL124-VAL142 | |
| B | MET146-PHE171 | |
| B | THR189-PHE204 | |
| B | ASN223-MET247 | |
| A | ILE41-LYS62 | |
| B | THR273-ALA301 | |
| B | ALA325-SER343 | |
| B | THR347-ALA370 | |
| B | PRO385-GLY404 | |
| B | GLU409-ASN427 | |
| A | PHE84-SER113 | |
| A | VAL124-VAL142 | |
| A | MET146-PHE171 | |
| A | THR189-PHE204 | |
| A | ASN223-MET247 | |
| A | THR273-ALA301 | |
| A | ALA325-SER343 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 138 |
| Details | TOPO_DOM: Periplasmic => ECO:0000255 |
| Chain | Residue | Details |
| A | GLY25-GLY40 | |
| B | GLY248-ASP272 | |
| B | PRO344-ALA346 | |
| B | SER405-LYS408 | |
| A | TYR114-LEU123 | |
| A | TRP172-GLY188 | |
| A | GLY248-ASP272 | |
| A | PRO344-ALA346 | |
| A | SER405-LYS408 | |
| B | GLY25-GLY40 | |
| B | TYR114-LEU123 | |
| B | TRP172-GLY188 |
| site_id | SWS_FT_FI4 |
| Number of Residues | 34 |
| Details | TOPO_DOM: Cytoplasmic => ECO:0000255, ECO:0000269|PubMed:15919996 |
| Chain | Residue | Details |
| A | TYR428-ASP445 | |
| B | TYR428-ASP445 |
| site_id | SWS_FT_FI5 |
| Number of Residues | 6 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:21368142, ECO:0007744|PDB:3OB6 |
| Chain | Residue | Details |
| A | ILE23 | |
| A | SER26 | |
| A | ALA96 | |
| B | ILE23 | |
| B | SER26 | |
| B | ALA96 |
| site_id | SWS_FT_FI6 |
| Number of Residues | 4 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:27582465, ECO:0007744|PDB:5J4N |
| Chain | Residue | Details |
| A | CYS97 | |
| A | ALA101 | |
| B | CYS97 | |
| B | ALA101 |
| site_id | SWS_FT_FI7 |
| Number of Residues | 6 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:27582465 |
| Chain | Residue | Details |
| A | MET104 | |
| A | SER203 | |
| A | TRP293 | |
| B | MET104 | |
| B | SER203 | |
| B | TRP293 |
| site_id | SWS_FT_FI8 |
| Number of Residues | 6 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:21368142 |
| Chain | Residue | Details |
| A | TRP202 | |
| A | ILE205 | |
| A | SER357 | |
| B | TRP202 | |
| B | ILE205 | |
| B | SER357 |
| site_id | SWS_FT_FI9 |
| Number of Residues | 6 |
| Details | SITE: Cytoplasmic (distal) gate => ECO:0000305|PubMed:27582465 |
| Chain | Residue | Details |
| A | TYR93 | |
| A | GLU208 | |
| A | TYR365 | |
| B | TYR93 | |
| B | GLU208 | |
| B | TYR365 |
| site_id | SWS_FT_FI10 |
| Number of Residues | 2 |
| Details | SITE: Periplasmic (proximal) gate => ECO:0000250|UniProtKB:P60063 |
| Chain | Residue | Details |
| A | TRP202 | |
| B | TRP202 |
| site_id | SWS_FT_FI11 |
| Number of Residues | 2 |
| Details | SITE: Middle gate => ECO:0000250|UniProtKB:P60063 |
| Chain | Residue | Details |
| A | TRP293 | |
| B | TRP293 |
