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3L1L

Structure of Arg-bound Escherichia coli AdiC

Functional Information from GO Data
ChainGOidnamespacecontents
A0005886cellular_componentplasma membrane
A0006865biological_processamino acid transport
A0015297molecular_functionantiporter activity
A0016020cellular_componentmembrane
A0022857molecular_functiontransmembrane transporter activity
A0042802molecular_functionidentical protein binding
A0055085biological_processtransmembrane transport
Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues110
DetailsTOPO_DOM: Cytoplasmic => ECO:0000255
ChainResidueDetails
AMET1-LEU12
ALYS62-GLY86
AGLY143
AGLU208-ILE226
ALYS302-PRO323
AALA371-LEU388
AASN427-ASP445

site_idSWS_FT_FI2
Number of Residues219
DetailsTRANSMEM: Helical => ECO:0007744|PDB:3L1L
ChainResidueDetails
AILE13-MET24
AVAL353-ALA370
AALA389-GLY404
ALYS408-LEU426
AILE43-ALA61
ATYR87-LEU112
ALEU125-VAL142
APRO144-PHE171
ASER195-VAL207
AALA227-MET247
AVAL278-ALA301
AVAL324-SER340

site_idSWS_FT_FI3
Number of Residues92
DetailsTOPO_DOM: Periplasmic => ECO:0000255
ChainResidueDetails
AGLY25-ALA42
ASER113-VAL124
ATRP172-GLN194
AGLY248-ILE277
ASER341-LEU352
ASER405-ALA407

site_idSWS_FT_FI4
Number of Residues7
DetailsBINDING: BINDING => ECO:0000269|PubMed:20090677, ECO:0007744|PDB:3L1L
ChainResidueDetails
AILE23
ASER26
AGLY27
AALA96
ACYS97
ATRP202
ATRP293

site_idSWS_FT_FI5
Number of Residues3
DetailsBINDING: BINDING => ECO:0000269|PubMed:20090677
ChainResidueDetails
AASN101
AILE205
ASER357

site_idSWS_FT_FI6
Number of Residues3
DetailsSITE: Cytoplasmic (distal) gate => ECO:0000305|PubMed:20090677
ChainResidueDetails
ATYR93
AGLU208
ATYR365

site_idSWS_FT_FI7
Number of Residues1
DetailsSITE: Periplasmic (proximal) gate => ECO:0000269|PubMed:20090677
ChainResidueDetails
ATRP202

site_idSWS_FT_FI8
Number of Residues1
DetailsSITE: Middle gate => ECO:0000305|PubMed:20090677
ChainResidueDetails
ATRP293

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PDB entries from 2024-07-10

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