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 | 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 | 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 | 500 |
| Details | Transmembrane: {"description":"Helical","evidences":[{"source":"PDB","id":"5J4I","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 322 |
| Details | Topological domain: {"description":"Periplasmic","evidences":[{"evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 310 |
| Details | Topological domain: {"description":"Cytoplasmic","evidences":[{"evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 14 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"20090677","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"3L1L","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI5 |
| Number of Residues | 6 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"20090677","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI6 |
| Number of Residues | 4 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"27582465","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI7 |
| Number of Residues | 6 |
| Details | Site: {"description":"Cytoplasmic (distal) gate","evidences":[{"source":"PubMed","id":"20090677","evidenceCode":"ECO:0000305"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI8 |
| Number of Residues | 2 |
| Details | Site: {"description":"Periplasmic (proximal) gate","evidences":[{"source":"PubMed","id":"20090677","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI9 |
| Number of Residues | 2 |
| Details | Site: {"description":"Middle gate","evidences":[{"source":"PubMed","id":"20090677","evidenceCode":"ECO:0000305"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI10 |
| Number of Residues | 438 |
| Details | Transmembrane: {"description":"Helical","evidences":[{"source":"PDB","id":"3L1L","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI11 |
| Number of Residues | 4 |
| Details | Motif: {"description":"Helix-breaking GSG motif TM1","evidences":[{"source":"PubMed","id":"19478139","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"20090677","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI12 |
| Number of Residues | 8 |
| Details | Motif: {"description":"Helix-breaking GVESA motif TM6","evidences":[{"source":"PubMed","id":"19478139","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"20090677","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
