3MPQ: I204R1 mutant of LeuT

Name: PDB 3MPQ: I204R1 mutant of LeuT
Published: 2010-12-01
License: https://creativecommons.org/publicdomain/zero/1.0/
Keywords: membrane protein

I204R1 mutant of LeuT. Determined by X-ray diffraction at 2.25 Å resolution. Released 1 Dec 2010.

Method: X-ray diffraction
Resolution: 2.25 Å
Organism: Aquifex aeolicus
Chains: 1
Atoms: 4,016
Mol. weight: 58.15 kDa
Ligands: MTN, LEU, BOG
Released: 1 Dec 2010

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

Secondary structure: helices and β-sheets

3MPQ contains 36 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: 36 helices, 4 β-strands

Element	Residues	Length	Sheet
α-helix	11-22	12
α-helix	25	1
α-helix	26-30	5
α-helix	31-37	7
α-helix	41-50	10
α-helix	51-55	5
α-helix	56-71	16
α-helix	77-84	8
α-helix	88-123	36
α-helix	137-152	16
β-strand	161	1	1
α-helix	166-184	19
α-helix	187-192	6
α-helix	193-214	22
β-strand	217-218	2	2
β-strand	221-222	2	2
α-helix	224-230	7
α-helix	237-239	3
α-helix	241-255	15
α-helix	261-266	6
α-helix	276-288	13
α-helix	289-294	6
α-helix	295-306	12
α-helix	308-317	10
α-helix	321	1
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	422-426	5
α-helix	429-437	9
α-helix	443-445	3
α-helix	447-450	4
α-helix	451-455	5
α-helix	456-465	10
α-helix	483-509	27

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Transporter	A	protein	507	Aquifex aeolicus	O67854 (AlphaFold model)

Sequence of entity 1 (A), FASTA

>3MPQ_1 Transporter (chains A)
KREHWATRLGLILAMAGNAVGLGNFLRFPVQAAENGGGAFMIPYIIAFLLVGIPLMWIEW
AMGRYGGAQGHGTTPAIFYLLWRNRFAKILGVFGLWIPLVVAIYYVYIESWTLGFAIKFL
VGLVPEPPPNATDPDSILRPFKEFLYSYIGVPKGDEPILKPSLFAYIVFLITMFINVSIL
IRGISKGIERFAKIAMPTLFCLAVFLVIRVFLLETPNGTAADGLNFLWTPDFEKLKDPGV
WIAAVGQIFFTLSLGFGAIITYASYVRKDQDIVLSGLTAATLNEKAEVILGGSISIPAAV
AFFGVANAVAIAKAGAFNLGFITLPAIFSQTAGGTFLGFLWFFLLFFAGLTSSIAIMQPM
IAFLEDELKLSRKHAVLWTAAIVFFSAHLVMFLNKSLDEMDFWAGTIGVVFFGLTELIIF
FWIFGADKAWEEINRGGIIKVPRIYYYVMRYITPAFLAVLLVVWAREYIPKIMEETHWTV
WITRFYIIGLFLFLTFLVFLAERRRNH

Ligands and cofactors

ID	Name	Formula	Copies
MTN	S-[(1-oxyl-2,2,5,5-tetramethyl-2,5-dihydro-1H-pyrrol-3-yl)methyl]…	C10 H18 N O3 S2	1
LEU	Leucine	C6 H13 N O2	1
BOG	octyl beta-D-glucopyranoside	C14 H28 O6	3

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

Primary citation

Structural origins of nitroxide side chain dynamics on membrane protein alpha-helical sites. Kroncke, B.M., Horanyi, P.S., Columbus, L. Biochemistry (2010) 49:10045-10060. DOI 10.1021/bi101148w · 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
3F3A 2.0 Å, Crystal Structure of LeuT bound to L-Tryptophan 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

Browse structure collections

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