7O82
The L-arginine/agmatine antiporter from E. coli at 1.7 A resolution
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 | 3 |
Details | binding site for residue BNG A 501 |
Chain | Residue |
A | ILE99 |
A | LEU352 |
A | HOH615 |
site_id | AC2 |
Number of Residues | 6 |
Details | binding site for residue TRS A 502 |
Chain | Residue |
A | TYR87 |
A | PRO311 |
A | ASN427 |
A | TYR428 |
A | HOH611 |
A | HOH703 |
site_id | AC3 |
Number of Residues | 1 |
Details | binding site for residue HEX A 503 |
Chain | Residue |
A | ILE13 |
site_id | AC4 |
Number of Residues | 2 |
Details | binding site for residue D10 A 504 |
Chain | Residue |
A | ARG149 |
A | VAL153 |
site_id | AC5 |
Number of Residues | 3 |
Details | binding site for residue BNG B 501 |
Chain | Residue |
B | LEU352 |
B | LYS408 |
B | TRP412 |
site_id | AC6 |
Number of Residues | 1 |
Details | binding site for residue BNG B 502 |
Chain | Residue |
B | MET179 |
site_id | AC7 |
Number of Residues | 5 |
Details | binding site for residue TRS B 503 |
Chain | Residue |
B | TYR87 |
B | PHE310 |
B | ASN427 |
B | TYR428 |
B | HOH704 |
site_id | AC8 |
Number of Residues | 2 |
Details | binding site for residue HEX B 505 |
Chain | Residue |
B | ARG316 |
B | ALA325 |
site_id | AC9 |
Number of Residues | 1 |
Details | binding site for residue HEX B 507 |
Chain | Residue |
B | TYR44 |
site_id | AD1 |
Number of Residues | 2 |
Details | binding site for residue HEX B 508 |
Chain | Residue |
A | ARG222 |
B | HOH756 |
site_id | AD2 |
Number of Residues | 1 |
Details | binding site for residue D10 B 509 |
Chain | Residue |
B | ARG149 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 388 |
Details | TOPO_DOM: Cytoplasmic => ECO:0000255 |
Chain | Residue | Details |
A | MET1-LEU12 | |
B | GLY143 | |
B | GLU208-ILE226 | |
B | LYS302-PRO323 | |
B | ALA371-LEU388 | |
B | ASN427-ASP445 | |
A | MET1-GLY11 | |
A | MET63-PRO83 | |
A | GLY143-LYS145 | |
A | ILE205-ARG222 | |
A | LYS302-VAL324 | |
A | LYS62-GLY86 | |
A | ALA371-ARG384 | |
B | MET1-GLY11 | |
B | MET63-PRO83 | |
B | GLY143-LYS145 | |
B | ILE205-ARG222 | |
B | LYS302-VAL324 | |
B | ALA371-ARG384 | |
A | GLY143 | |
A | GLU208-ILE226 | |
A | LYS302-PRO323 | |
A | ALA371-LEU388 | |
A | ASN427-ASP445 | |
B | MET1-LEU12 | |
B | LYS62-GLY86 |
site_id | SWS_FT_FI2 |
Number of Residues | 438 |
Details | TRANSMEM: Helical => ECO:0007744|PDB:3L1L |
Chain | Residue | Details |
A | ILE13-MET24 | |
A | VAL353-ALA370 | |
A | ALA389-GLY404 | |
A | LYS408-LEU426 | |
B | ILE13-MET24 | |
B | ILE43-ALA61 | |
B | TYR87-LEU112 | |
B | LEU125-VAL142 | |
B | PRO144-PHE171 | |
B | SER195-VAL207 | |
B | ALA227-MET247 | |
A | ILE43-ALA61 | |
B | VAL278-ALA301 | |
B | VAL324-SER340 | |
B | VAL353-ALA370 | |
B | ALA389-GLY404 | |
B | LYS408-LEU426 | |
A | TYR87-LEU112 | |
A | LEU125-VAL142 | |
A | PRO144-PHE171 | |
A | SER195-VAL207 | |
A | ALA227-MET247 | |
A | VAL278-ALA301 | |
A | VAL324-SER340 |
site_id | SWS_FT_FI3 |
Number of Residues | 322 |
Details | TOPO_DOM: Periplasmic => ECO:0000255 |
Chain | Residue | Details |
A | GLY25-ALA42 | |
B | GLY248-ILE277 | |
B | SER341-LEU352 | |
B | SER405-ALA407 | |
A | GLY25-GLY40 | |
A | TYR114-LEU123 | |
A | TRP172-GLY188 | |
A | GLY248-ASP272 | |
A | PRO344-ALA346 | |
A | SER405-LYS408 | |
B | GLY25-GLY40 | |
A | SER113-VAL124 | |
B | TYR114-LEU123 | |
B | TRP172-GLY188 | |
B | GLY248-ASP272 | |
B | PRO344-ALA346 | |
B | SER405-LYS408 | |
A | TRP172-GLN194 | |
A | GLY248-ILE277 | |
A | SER341-LEU352 | |
A | SER405-ALA407 | |
B | GLY25-ALA42 | |
B | SER113-VAL124 | |
B | TRP172-GLN194 |
site_id | SWS_FT_FI4 |
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_FI5 |
Number of Residues | 2 |
Details | BINDING: BINDING => ECO:0000269|PubMed:20090677, ECO:0007744|PDB:3L1L |
Chain | Residue | Details |
A | GLY27 | |
B | GLY27 |
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 | ASN101 | |
B | CYS97 | |
B | ASN101 |
site_id | SWS_FT_FI7 |
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_FI8 |
Number of Residues | 6 |
Details | BINDING: BINDING => ECO:0000269|PubMed:27582465 |
Chain | Residue | Details |
A | TRP293 | |
B | TRP293 | |
A | MET104 | |
A | SER203 | |
B | MET104 | |
B | SER203 |
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 |
site_id | SWS_FT_FI12 |
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_FI13 |
Number of Residues | 34 |
Details | TOPO_DOM: Cytoplasmic => ECO:0000255, ECO:0000269|PubMed:15919996 |
Chain | Residue | Details |
A | TYR428-ASP445 | |
B | TYR428-ASP445 |