Structure of PDB 3hfx Chain A

Receptor sequence
>3hfxA (length=493) Species: 83333 (Escherichia coli K-12) [Search protein sequence]
PKVFFPPLIIVGILCWLTVRDLDAANVVINAVFSYVTNVWGWAFEWYMVV
MLFGWFWLVFGPYAKKRLGNEPPEFSTASWIFMMFASCTSAAVLFWGSIE
IYYYISTPPFGLEPNSTGAKELGLAYSLFHWGPLPWATYSFLSVAFAYFF
FVRKMEVIRPSSTLVPLVGEKHAKGLFGTIVDNFYLVALIFAMGTSLGLA
TPLVTECMQWLFGIPHTLQLDAIIITCWIILNAICVACGLQKGVRIASDV
RSYLSFLMLGWVFIVSGASFIMNYFTDSVGMLLMYLPRMLFYTDPIAKGG
FPQGWTVFYWAWWVIYAIQMSIFLARISRGRTVRELCFGMVLGLTASTWI
LWTVLGSNTLLLIDKNIINIPNLIEQYGVARAIIETWAALPLSTATMWGF
FILCFIATVTLVNACSYTLAMSTCREVRDGEEPPLLVRIGWSILVGIIGI
VLLALGGLKPIQTAIIAGGCPLFFVNIMVTLSFIKDAKQNWKD
3D structure
PDB3hfx Crystal structure of the carnitine transporter and insights into the antiport mechanism
ChainA
Resolution3.15 Å
3D
structure
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Enzymatic activity
Enzyme Commision number ?
Interaction with ligand
Site
#		 Ligand Ligand
chain		 Binding residues on receptor
(original residue number in PDB)		 Binding residues on receptor
(residue number reindexed from 1)		 Binding affinity
BS01 152 A W142 W323 W324 Y327 W131 W312 W313 Y316
BS02 152 A Y327 Q330 F334 Y316 Q319 F323
BS03 152 A Y114 W316 Y103 W305
Gene Ontology
Molecular Function
GO:0015226 carnitine transmembrane transporter activity
GO:0015297 antiporter activity
GO:0022857 transmembrane transporter activity
GO:0044667 (R)-carnitine:4-(trimethylammonio)butanoate antiporter activity
Biological Process
GO:0009437 carnitine metabolic process
GO:0015879 carnitine transport
GO:0071705 nitrogen compound transport
GO:1900749 (R)-carnitine transport
GO:1900751 4-(trimethylammonio)butanoate transport
GO:1902270 (R)-carnitine transmembrane transport
GO:1902603 carnitine transmembrane transport
Cellular Component
GO:0005886 plasma membrane
GO:0016020 membrane

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Molecular Function
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Biological Process
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Cellular Component
External links
PDB RCSB:3hfx, PDBe:3hfx, PDBj:3hfx
PDBsum3hfx
PubMed20357772
UniProtP31553|CAIT_ECOLI L-carnitine/gamma-butyrobetaine antiporter (Gene Name=caiT)

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