F177R1 mutant of LeuT. Determined by X-ray diffraction at 2.25 Å resolution. Released 1 Dec 2010.
Explore 3MPN in 3D Show helices and sheets RCSB PDB PDBe
3MPN contains 38 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.
| 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 | 88-94 | 7 | |
| α-helix | 96-124 | 29 | |
| α-helix | 128-131 | 4 | |
| 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 | 223-231 | 9 | |
| α-helix | 237-239 | 3 | |
| α-helix | 241-255 | 15 | |
| α-helix | 261-266 | 6 | |
| α-helix | 276-287 | 12 | |
| α-helix | 288-294 | 7 | |
| α-helix | 295-306 | 12 | |
| α-helix | 308-317 | 10 | |
| α-helix | 321-326 | 6 | |
| 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 | 456-470 | 15 | |
| α-helix | 472-477 | 6 | |
| α-helix | 483-509 | 27 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Transporter | A | protein | 507 | Aquifex aeolicus | O67854 (AlphaFold model) |
>3MPN_1 Transporter (chains A) REHWATRLGLILAMAGNAVGLGNFLRFPVQAAENGGGAFMIPYIIAFLLVGIPLMWIEWA MGRYGGAQGHGTTPAIFYLLWRNRFAKILGVFGLWIPLVVAIYYVYIESWTLGFAIKFLV GLVPEPPPNATDPDSILRPFKEFLYSYIGVPKGDEPILKPSLFAYIVFLITMCINVSILI RGISKGIERFAKIAMPTLFILAVFLVIRVFLLETPNGTAADGLNFLWTPDFEKLKDPGVW IAAVGQIFFTLSLGFGAIITYASYVRKDQDIVLSGLTAATLNEKAEVILGGSISIPAAVA FFGVANAVAIAKAGAFNLGFITLPAIFSQTAGGTFLGFLWFFLLFFAGLTSSIAIMQPMI AFLEDELKLSRKHAVLWTAAIVFFSAHLVMFLNKSLDEMDFWAGTIGVVFFGLTELIIFF WIFGADKAWEEINRGGIIKVPRIYYYVMRYITPAFLAVLLVVWAREYIPKIMEETHWTVW ITRFYIIGLFLFLTFLVFLAERRRNHE
| ID | Name | Formula | Copies |
|---|---|---|---|
| LEU | Leucine | C6 H13 N O2 | 1 |
| MTN | S-[(1-oxyl-2,2,5,5-tetramethyl-2,5-dihydro-1H-pyrrol-3-yl)methyl]… | C10 H18 N O3 S2 | 1 |
| BOG | octyl beta-D-glucopyranoside | C14 H28 O6 | 6 |
Water and common crystallization additives (NA, CL) are not listed.
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:
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