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2WSX

Crystal Structure of Carnitine Transporter from Escherichia coli

Functional Information from GO Data
ChainGOidnamespacecontents
A0005886cellular_componentplasma membrane
A0009437biological_processcarnitine metabolic process
A0015226molecular_functioncarnitine transmembrane transporter activity
A0015297molecular_functionantiporter activity
A0015879biological_processcarnitine transport
A0016020cellular_componentmembrane
A0022857molecular_functiontransmembrane transporter activity
A0044667molecular_function(R)-carnitine:4-(trimethylammonio)butanoate antiporter activity
A0071705biological_processnitrogen compound transport
A1900749biological_process(R)-carnitine transport
A1900751biological_process4-(trimethylammonio)butanoate transport
A1902270biological_process(R)-carnitine transmembrane transport
A1902603biological_processcarnitine transmembrane transport
B0005886cellular_componentplasma membrane
B0009437biological_processcarnitine metabolic process
B0015226molecular_functioncarnitine transmembrane transporter activity
B0015297molecular_functionantiporter activity
B0015879biological_processcarnitine transport
B0016020cellular_componentmembrane
B0022857molecular_functiontransmembrane transporter activity
B0044667molecular_function(R)-carnitine:4-(trimethylammonio)butanoate antiporter activity
B0071705biological_processnitrogen compound transport
B1900749biological_process(R)-carnitine transport
B1900751biological_process4-(trimethylammonio)butanoate transport
B1902270biological_process(R)-carnitine transmembrane transport
B1902603biological_processcarnitine transmembrane transport
C0005886cellular_componentplasma membrane
C0009437biological_processcarnitine metabolic process
C0015226molecular_functioncarnitine transmembrane transporter activity
C0015297molecular_functionantiporter activity
C0015879biological_processcarnitine transport
C0016020cellular_componentmembrane
C0022857molecular_functiontransmembrane transporter activity
C0044667molecular_function(R)-carnitine:4-(trimethylammonio)butanoate antiporter activity
C0071705biological_processnitrogen compound transport
C1900749biological_process(R)-carnitine transport
C1900751biological_process4-(trimethylammonio)butanoate transport
C1902270biological_process(R)-carnitine transmembrane transport
C1902603biological_processcarnitine transmembrane transport
Functional Information from PDB Data
site_idAC1
Number of Residues4
DetailsBINDING SITE FOR RESIDUE NM2 A 1504
ChainResidue
ATRP142
ATRP323
ATYR327
AMET331

site_idAC2
Number of Residues5
DetailsBINDING SITE FOR RESIDUE NM2 A 1505
ChainResidue
AGLY311
APHE312
AGLY315
ALEU469
AGLN473

site_idAC3
Number of Residues4
DetailsBINDING SITE FOR RESIDUE NM2 B 1504
ChainResidue
BTRP142
BTRP323
BTYR327
BMET331

site_idAC4
Number of Residues5
DetailsBINDING SITE FOR RESIDUE NM2 B 1505
ChainResidue
BTYR114
BGLY311
BPHE312
BGLY315
BGLN473

site_idAC5
Number of Residues4
DetailsBINDING SITE FOR RESIDUE NM2 C 1504
ChainResidue
CTRP142
CTRP323
CTYR327
CMET331

site_idAC6
Number of Residues6
DetailsBINDING SITE FOR RESIDUE NM2 C 1505
ChainResidue
CTYR114
CGLY311
CPHE312
CGLY315
CLEU469
CGLN473

Functional Information from PROSITE/UniProt
site_idPS01303
Number of Residues10
DetailsBCCT BCCT family of transporters signature. GWTVfYWaWW
ChainResidueDetails
AGLY315-TRP324

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues333
DetailsTOPO_DOM: Cytoplasmic => ECO:0000269|PubMed:20357772, ECO:0007744|PDB:3HFX
ChainResidueDetails
AMET1-PRO12
BPHE152-GLY186
BCYS249-LYS253
BALA336-PHE349
BMET432-LEU446
BTHR491-ASP504
CMET1-PRO12
CTRP68-SER90
CPHE152-GLY186
CCYS249-LYS253
CALA336-PHE349
ATRP68-SER90
CMET432-LEU446
CTHR491-ASP504
APHE152-GLY186
ACYS249-LYS253
AALA336-PHE349
AMET432-LEU446
ATHR491-ASP504
BMET1-PRO12
BTRP68-SER90

site_idSWS_FT_FI2
Number of Residues726
DetailsTRANSMEM: Helical => ECO:0000269|PubMed:20357772, ECO:0007744|PDB:3HFX
ChainResidueDetails
ALYS13-VAL30
ASER404-ALA431
ALEU447-LEU466
ALEU469-VAL490
BLYS13-VAL30
BGLY52-PHE67
BTRP91-SER98
BGLU132-SER151
BLEU187-MET219
BLEU231-ALA248
BALA254-SER277
AGLY52-PHE67
BPHE312-LEU335
BGLY350-LEU372
BSER404-ALA431
BLEU447-LEU466
BLEU469-VAL490
CLYS13-VAL30
CGLY52-PHE67
CTRP91-SER98
CGLU132-SER151
CLEU187-MET219
ATRP91-SER98
CLEU231-ALA248
CALA254-SER277
CPHE312-LEU335
CGLY350-LEU372
CSER404-ALA431
CLEU447-LEU466
CLEU469-VAL490
AGLU132-SER151
ALEU187-MET219
ALEU231-ALA248
AALA254-SER277
APHE312-LEU335
AGLY350-LEU372

site_idSWS_FT_FI3
Number of Residues378
DetailsTOPO_DOM: Periplasmic => ECO:0000269|PubMed:20357772, ECO:0007744|PDB:3HFX
ChainResidueDetails
AARG31-TRP51
BGLY278-GLY311
BLEU373-LEU403
BGLY467-GLY468
CARG31-TRP51
CCYS99-LYS131
CGLN220-GLN230
CGLY278-GLY311
CLEU373-LEU403
CGLY467-GLY468
ACYS99-LYS131
AGLN220-GLN230
AGLY278-GLY311
ALEU373-LEU403
AGLY467-GLY468
BARG31-TRP51
BCYS99-LYS131
BGLN220-GLN230

site_idSWS_FT_FI4
Number of Residues12
DetailsBINDING: BINDING => ECO:0000269|PubMed:20829798, ECO:0007744|PDB:2WSX
ChainResidueDetails
ATYR114
CGLY315
CTRP323
CMET331
AGLY315
ATRP323
AMET331
BTYR114
BGLY315
BTRP323
BMET331
CTYR114

site_idSWS_FT_FI5
Number of Residues6
DetailsBINDING: BINDING => ECO:0000269|PubMed:20357772, ECO:0007744|PDB:3HFX
ChainResidueDetails
ATRP142
ATYR327
BTRP142
BTYR327
CTRP142
CTYR327

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PDB entries from 2025-06-11

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