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3HFX

Crystal structure of carnitine transporter

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
Functional Information from PDB Data
site_idAC1
Number of Residues1
DetailsBINDING SITE FOR RESIDUE HG A 505
ChainResidue
ACYS481

site_idAC2
Number of Residues3
DetailsBINDING SITE FOR RESIDUE HG A 506
ChainResidue
ACYS99
ATHR100
ASER101

site_idAC3
Number of Residues2
DetailsBINDING SITE FOR RESIDUE HG A 507
ChainResidue
ACYS238
ALEU242

site_idAC4
Number of Residues3
DetailsBINDING SITE FOR RESIDUE HG A 508
ChainResidue
ACYS26
AILE459
AVAL462

site_idAC5
Number of Residues3
DetailsBINDING SITE FOR RESIDUE HG A 509
ChainResidue
AMET204
ALEU422
ACYS426

site_idAC6
Number of Residues6
DetailsBINDING SITE FOR RESIDUE HG A 510
ChainResidue
ALEU214
AVAL215
ACYS218
APHE411
APHE412
ACYS415

site_idAC7
Number of Residues3
DetailsBINDING SITE FOR RESIDUE HG A 511
ChainResidue
AMET204
ACYS426
A152602

site_idAC8
Number of Residues3
DetailsBINDING SITE FOR RESIDUE HG A 512
ChainResidue
ALEU251
AGLN252
AVAL255

site_idAC9
Number of Residues2
DetailsBINDING SITE FOR RESIDUE HG A 513
ChainResidue
AALA248
ACYS249

site_idBC1
Number of Residues5
DetailsBINDING SITE FOR RESIDUE 152 A 601
ChainResidue
ASER101
AVAL104
ATRP323
ATRP324
ATYR327

site_idBC2
Number of Residues6
DetailsBINDING SITE FOR RESIDUE 152 A 602
ChainResidue
ATYR327
AGLN330
AMET331
APHE334
ALEU422
AHG511

site_idBC3
Number of Residues4
DetailsBINDING SITE FOR RESIDUE 152 A 603
ChainResidue
ATYR114
AGLY310
AGLY311
ATRP316

site_idBC4
Number of Residues4
DetailsBINDING SITE FOR RESIDUE 152 A 604
ChainResidue
AGLU85
APHE86
AARG337
AILE338

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 Residues242
DetailsTransmembrane: {"description":"Helical","evidences":[{"source":"PubMed","id":"20357772","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"3HFX","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues126
DetailsTopological domain: {"description":"Periplasmic","evidences":[{"source":"PubMed","id":"20357772","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"3HFX","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues100
DetailsTopological domain: {"description":"Cytoplasmic","evidences":[{"source":"PubMed","id":"20357772","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"3HFX","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues4
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"20829798","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"2WSX","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI5
Number of Residues5
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"20357772","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"3HFX","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

238895

PDB entries from 2025-07-16

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