3F3A: LeuT

Crystal Structure of LeuT bound to L-Tryptophan and Sodium. Determined by X-ray diffraction at 2.0 Å resolution. Released 23 Dec 2008.

Method: X-ray diffraction
Resolution: 2.0 Å
Organism: Aquifex aeolicus
Chains: 1
Atoms: 4,327
Mol. weight: 61.19 kDa
Ligands: TRP, BOG, C14
Released: 23 Dec 2008

Explore 3F3A in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

3F3A contains 39 α-helices and 4 β-strands across 1 chain. Residue ranges use author residue numbering, as in the PDB file, from PDBe. To see them in 3D, choose the Cartoon representation with Secondary structure coloring: helices, sheets and coils get different colors.

Chain A: 39 helices, 4 β-strands

Element	Residues	Length	Sheet
α-helix	11-22	12
α-helix	25-28	4
α-helix	30-37	8
α-helix	40-43	4
α-helix	44-50	7
α-helix	51-55	5
α-helix	56-71	16
α-helix	77-84	8
α-helix	88-124	37
α-helix	137-152	16
β-strand	161	1	1
α-helix	166-183	18
α-helix	186	1
α-helix	187-192	6
α-helix	193-215	23
β-strand	217-218	2	2
β-strand	221-222	2	2
α-helix	223-231	9
α-helix	235-239	5
α-helix	241-254	14
α-helix	261-266	6
α-helix	276-287	12
α-helix	288-294	7
α-helix	298-306	9
α-helix	308-310	3
α-helix	311-316	6
α-helix	319-321	3
α-helix	322-326	5
α-helix	327-331	5
α-helix	337-371	35
α-helix	375-395	21
β-strand	396	1	1
α-helix	399-405	7
α-helix	406-411	6
α-helix	412-421	10
α-helix	422-427	6
α-helix	429-437	9
α-helix	443-445	3
α-helix	448-450	3
α-helix	451-455	5
α-helix	456-469	14
α-helix	472-477	6
α-helix	483-510	28

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Transporter	A	protein	519	Aquifex aeolicus	O67854 (AlphaFold model)

Sequence of entity 1 (A), FASTA

>3F3A_1 Transporter (chains A)
MEVKREHWATRLGLILAMAGNAVGLGNFLRFPVQAAENGGGAFMIPYIIAFLLVGIPLMW
IEWAMGRYGGAQGHGTTPAIFYLLWRNRFAKILGVFGLWIPLVVAIYYVYIESWTLGFAI
KFLVGLVPEPPPNATDPDSILRPFKEFLYSYIGVPKGDEPILKPSLFAYIVFLITMFINV
SILIRGISKGIERFAKIAMPTLFILAVFLVIRVFLLETPNGTAADGLNFLWTPDFEKLKD
PGVWIAAVGQIFFTLSLGFGAIITYASYVRKDQDIVLSGLTAATLNEKAEVILGGSISIP
AAVAFFGVANAVAIAKAGAFNLGFITLPAIFSQTAGGTFLGFLWFFLLFFAGLTSSIAIM
QPMIAFLEDELKLSRKHAVLWTAAIVFFSAHLVMFLNKSLDEMDFWAGTIGVVFFGLTEL
IIFFWIFGADKAWEEINRGGIIKVPRIYYYVMRYITPAFLAVLLVVWAREYIPKIMEETH
WTVWITRFYIIGLFLFLTFLVFLAERRRNHESAGTLVPR

Ligands and cofactors

ID	Name	Formula	Copies
TRP	Tryptophan	C11 H12 N2 O2	4
BOG	octyl beta-D-glucopyranoside	C14 H28 O6	7
C14	Tetradecane	C14 H30	1

Water and common crystallization additives (NA) are not listed.

Primary citation

A competitive inhibitor traps LeuT in an open-to-out conformation. Singh, S.K., Piscitelli, C.L., Yamashita, A. et al. Science (2008) 322:1655-1661. DOI 10.1126/science.1166777 · PubMed

Other PDB entries of the same protein (UniProt O67854 (AlphaFold model), which also has an AlphaFold model), best resolution first:

2A65 1.65 Å, Crystal structure of LEUTAA, a bacterial homolog of Na+/Cl--dependent neurotransmitter…
2Q72 1.7 Å, Crystal Structure Analysis of LeuT complexed with L-leucine, sodium, and imipramine
3F3E 1.8 Å, Crystal structure of LeuT bound to L-leucine (30 mM) and sodium
2Q6H 1.85 Å, Crystal Structure Analysis of LeuT complexed with L-leucine, sodium, and clomipramine
2QEI 1.85 Å, Crystal structure analysis of LeuT complexed with L-alanine, sodium, and clomipramine
2QB4 1.9 Å, Crystal Structure Analysis of LeuT complexed with L-leucine, sodium and desipramine
3F48 1.9 Å, Crystal structure of LeuT bound to L-alanine and sodium
3F4I 1.95 Å, Crystal Structure of LeuT bound to L-selenomethionine and sodium
3GJD 2.0 Å, Crystal Structure of LeuT with bound OG
3F3C 2.1 Å, Crystal structure of LeuT bound to 4-Fluoro-L-Phenylalanine and sodium
3USP 2.1 Å, Crystal structure of LeuT in heptyl-beta-D-Selenoglucoside
7LQK 2.1 Å, Crystal structure of the R375A mutant of LeuT

Browse structure collections

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