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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
A0015695biological_processorganic cation transport
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
B0015695biological_processorganic cation transport
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 Residues388
DetailsTOPO_DOM: Cytoplasmic => ECO:0000255
ChainResidueDetails
ALYS62-GLY86
AGLU208-ILE226
ALYS302-PRO323
AALA371-LEU388
AASN427-ASP445
BMET1-LEU12
BLYS62-GLY86
BGLU208-ILE226
BLYS302-PRO323
BALA371-LEU388
BASN427-ASP445
AMET1-GLY11
AMET63-PRO83
AGLY143-LYS145
AILE205-ARG222
ALYS302-VAL324
AALA371-ARG384
BMET1-GLY11
BMET63-PRO83
BGLY143-LYS145
BILE205-ARG222
BLYS302-VAL324
BALA371-ARG384
AGLY143
BGLY143
AMET1-LEU12

site_idSWS_FT_FI2
Number of Residues438
DetailsTRANSMEM: Helical => ECO:0007744|PDB:3L1L
ChainResidueDetails
AILE13-MET24
AILE43-ALA61
ATYR87-LEU112
ALEU125-VAL142
APRO144-PHE171
ASER195-VAL207
AALA227-MET247
AVAL278-ALA301
AVAL324-SER340
AVAL353-ALA370
AALA389-GLY404
ALYS408-LEU426
BILE13-MET24
BILE43-ALA61
BTYR87-LEU112
BLEU125-VAL142
BPRO144-PHE171
BSER195-VAL207
BALA227-MET247
BVAL278-ALA301
BVAL324-SER340
BVAL353-ALA370
BALA389-GLY404
BLYS408-LEU426

site_idSWS_FT_FI3
Number of Residues322
DetailsTOPO_DOM: Periplasmic => ECO:0000255
ChainResidueDetails
AGLY25-ALA42
ASER113-VAL124
ATRP172-GLN194
AGLY248-ILE277
ASER341-LEU352
ASER405-ALA407
BGLY25-ALA42
BSER113-VAL124
BTRP172-GLN194
BGLY248-ILE277
BSER341-LEU352
BSER405-ALA407
AGLY25-GLY40
ATYR114-LEU123
ATRP172-GLY188
AGLY248-ASP272
APRO344-ALA346
ASER405-LYS408
BGLY25-GLY40
BTYR114-LEU123
BTRP172-GLY188
BGLY248-ASP272
BPRO344-ALA346
BSER405-LYS408

site_idSWS_FT_FI4
Number of Residues6
DetailsBINDING: BINDING => ECO:0000269|PubMed:21368142, ECO:0007744|PDB:3OB6
ChainResidueDetails
BSER26
BALA96
AILE23
ASER26
AALA96
BILE23

site_idSWS_FT_FI5
Number of Residues2
DetailsBINDING: BINDING => ECO:0000269|PubMed:20090677, ECO:0007744|PDB:3L1L
ChainResidueDetails
AGLY27
BGLY27

site_idSWS_FT_FI6
Number of Residues4
DetailsBINDING: BINDING => ECO:0000269|PubMed:27582465, ECO:0007744|PDB:5J4N
ChainResidueDetails
BCYS97
BASN101
AASN101
ACYS97

site_idSWS_FT_FI7
Number of Residues6
DetailsBINDING: BINDING => ECO:0000269|PubMed:21368142
ChainResidueDetails
ASER357
BTRP202
BILE205
BSER357
ATRP202
AILE205

site_idSWS_FT_FI8
Number of Residues6
DetailsBINDING: BINDING => ECO:0000269|PubMed:27582465
ChainResidueDetails
AMET104
ASER203
BMET104
BSER203
ATRP293
BTRP293

site_idSWS_FT_FI9
Number of Residues6
DetailsSITE: Cytoplasmic (distal) gate => ECO:0000305|PubMed:27582465
ChainResidueDetails
BGLU208
BTYR365
ATYR93
AGLU208
ATYR365
BTYR93

site_idSWS_FT_FI10
Number of Residues2
DetailsSITE: Periplasmic (proximal) gate => ECO:0000250|UniProtKB:P60063
ChainResidueDetails
ATRP202
BTRP202

site_idSWS_FT_FI11
Number of Residues2
DetailsSITE: Middle gate => ECO:0000250|UniProtKB:P60063
ChainResidueDetails
ATRP293
BTRP293

site_idSWS_FT_FI12
Number of Residues500
DetailsTRANSMEM: Helical => ECO:0007744|PDB:5J4I
ChainResidueDetails
AASN223-MET247
ATHR273-ALA301
AALA325-SER343
ATHR347-ALA370
APRO385-GLY404
AGLU409-ASN427
BLEU12-MET24
BILE41-LYS62
BPHE84-SER113
BVAL124-VAL142
BMET146-PHE171
BTHR189-PHE204
BASN223-MET247
BTHR273-ALA301
BALA325-SER343
BTHR347-ALA370
BPRO385-GLY404
BGLU409-ASN427
APHE84-SER113
AVAL124-VAL142
AMET146-PHE171
ATHR189-PHE204
ALEU12-MET24
AILE41-LYS62

site_idSWS_FT_FI13
Number of Residues34
DetailsTOPO_DOM: Cytoplasmic => ECO:0000255, ECO:0000269|PubMed:15919996
ChainResidueDetails
ATYR428-ASP445
BTYR428-ASP445

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PDB entries from 2024-06-12

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