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5J4I

Crystal Structure of the L-arginine/agmatine antiporter from E. coli at 2.2 Angstroem resolution

Functional Information from GO Data
ChainGOidnamespacecontents
A0003333biological_processamino acid transmembrane transport
A0005886cellular_componentplasma membrane
A0006865biological_processamino acid transport
A0015297molecular_functionantiporter activity
A0016020cellular_componentmembrane
A0022857molecular_functiontransmembrane transporter activity
A0043862molecular_functionarginine:agmatine antiporter activity
A0055085biological_processtransmembrane transport
A1905039biological_processcarboxylic acid transmembrane transport
A1990451biological_processcellular stress response to acidic pH
B0003333biological_processamino acid transmembrane transport
B0005886cellular_componentplasma membrane
B0006865biological_processamino acid transport
B0015297molecular_functionantiporter activity
B0016020cellular_componentmembrane
B0022857molecular_functiontransmembrane transporter activity
B0043862molecular_functionarginine:agmatine antiporter activity
B0055085biological_processtransmembrane transport
B1905039biological_processcarboxylic acid transmembrane transport
B1990451biological_processcellular stress response to acidic pH
Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues500
DetailsTransmembrane: {"description":"Helical","evidences":[{"source":"PDB","id":"5J4I","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues322
DetailsTopological domain: {"description":"Periplasmic","evidences":[{"evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues310
DetailsTopological domain: {"description":"Cytoplasmic","evidences":[{"evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues14
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"20090677","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"3L1L","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI5
Number of Residues6
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"20090677","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI6
Number of Residues4
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"27582465","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI7
Number of Residues6
DetailsSite: {"description":"Cytoplasmic (distal) gate","evidences":[{"source":"PubMed","id":"20090677","evidenceCode":"ECO:0000305"}]}
ChainResidueDetails

site_idSWS_FT_FI8
Number of Residues2
DetailsSite: {"description":"Periplasmic (proximal) gate","evidences":[{"source":"PubMed","id":"20090677","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI9
Number of Residues2
DetailsSite: {"description":"Middle gate","evidences":[{"source":"PubMed","id":"20090677","evidenceCode":"ECO:0000305"}]}
ChainResidueDetails

site_idSWS_FT_FI10
Number of Residues438
DetailsTransmembrane: {"description":"Helical","evidences":[{"source":"PDB","id":"3L1L","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI11
Number of Residues4
DetailsMotif: {"description":"Helix-breaking GSG motif TM1","evidences":[{"source":"PubMed","id":"19478139","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"20090677","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI12
Number of Residues8
DetailsMotif: {"description":"Helix-breaking GVESA motif TM6","evidences":[{"source":"PubMed","id":"19478139","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"20090677","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

247947

PDB entries from 2026-01-21

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