Overall structure of the LAT1-4F2hc bound with Leu. Determined by electron microscopy at 3.1 Å resolution. Released 13 Nov 2024.
Explore 8X0W in 3D Show helices and sheets RCSB PDB PDBe
8X0W contains 50 α-helices and 22 β-strands across 2 chains. 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 | 167-173 | 7 | |
| α-helix | 177-206 | 30 | |
| α-helix | 209-211 | 3 | |
| α-helix | 219-221 | 3 | |
| β-strand | 225-229 | 5 | 1 |
| α-helix | 231-235 | 5 | |
| α-helix | 242-248 | 7 | |
| α-helix | 249-255 | 7 | |
| β-strand | 261-262 | 2 | 1 |
| α-helix | 263-264 | 2 | |
| β-strand | 266 | 1 | 2 |
| α-helix | 280 | 1 | |
| β-strand | 281 | 1 | 2 |
| α-helix | 282 | 1 | |
| α-helix | 288-301 | 14 | |
| β-strand | 306-308 | 3 | 1 |
| α-helix | 325-341 | 17 | |
| β-strand | 346-349 | 4 | 1 |
| α-helix | 351-353 | 3 | |
| α-helix | 357-371 | 15 | |
| β-strand | 377-380 | 4 | 1 |
| α-helix | 386-392 | 7 | |
| β-strand | 400-402 | 3 | 1 |
| α-helix | 413-427 | 15 | |
| β-strand | 433-434 | 2 | 3 |
| α-helix | 442-444 | 3 | |
| α-helix | 451-458 | 8 | |
| β-strand | 464-465 | 2 | 3 |
| β-strand | 466-468 | 3 | 1 |
| α-helix | 488-490 | 3 | |
| α-helix | 506-508 | 3 | |
| α-helix | 510-513 | 4 | |
| α-helix | 520-533 | 14 | |
| α-helix | 535-539 | 5 | |
| β-strand | 543-544 | 2 | 4 |
| β-strand | 551-556 | 6 | 4 |
| β-strand | 563-569 | 7 | 4 |
| β-strand | 575-576 | 2 | 5 |
| α-helix | 586-588 | 3 | |
| β-strand | 593-594 | 2 | 6 |
| β-strand | 595 | 1 | 4 |
| β-strand | 610-611 | 2 | 6 |
| β-strand | 616-617 | 2 | 5 |
| α-helix | 618 | 1 | |
| β-strand | 622-627 | 6 | 4 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 50 | 1 | 7 |
| α-helix | 52-63 | 12 | |
| α-helix | 67-79 | 13 | |
| α-helix | 82-109 | 28 | |
| α-helix | 118-123 | 6 | |
| α-helix | 127-135 | 9 | |
| α-helix | 136-140 | 5 | |
| α-helix | 141-156 | 16 | |
| α-helix | 165-167 | 3 | |
| α-helix | 168-188 | 21 | |
| α-helix | 191-220 | 30 | |
| α-helix | 240-253 | 14 | |
| α-helix | 259-261 | 3 | |
| β-strand | 267 | 1 | 7 |
| α-helix | 270-297 | 28 | |
| α-helix | 302-307 | 6 | |
| α-helix | 311-320 | 10 | |
| α-helix | 326-354 | 29 | |
| α-helix | 374-385 | 12 | |
| α-helix | 386-388 | 3 | |
| α-helix | 394-397 | 4 | |
| α-helix | 401-421 | 21 | |
| α-helix | 435-452 | 18 | |
| α-helix | 456-466 | 11 | |
| α-helix | 468-472 | 5 | |
| α-helix | 473-477 | 5 | |
| α-helix | 483-500 | 18 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Amino acid transporter heavy chain SLC3A2 | A | protein | 470 | Homo sapiens | P08195 (AlphaFold model) |
| Large neutral amino acids transporter small subunit 1 | B | protein | 464 | Homo sapiens | Q01650 (AlphaFold model) |
>8X0W_1 Amino acid transporter heavy chain SLC3A2 (chains A) FTGLSKEELLKVAGSPGWVRTRWALLLLFWLGWLGMLAGAVVIIVRAPRCRELPAQKWWH TGALYRIGDLQAFQGHGAGNLAGLKGRLDYLSSLKVKGLVLGPIHKNQKDDVAQTDLLQI DPNFGSKEDFDSLLQSAKKKSIRVILDLTPNYRGENSWFSTQVDTVATKVKDALEFWLQA GVDGFQVRDIENLKDASSFLAEWQNITKGFSEDRLLIAGTNSSDLQQILSLLESNKDLLL TSSYLSDSGSTGEHTKSLVTQYLNATGNRWCSWSLSQARLLTSFLPAQLLRLYQLMLFTL PGTPVFSYGDEIGLDAAALPGQPMEAPVMLWDESSFPDIPGAVSANMTVKGQSEDPGSLL SLFRRLSDQRSKERSLLHGDFHAFSAGPGLFSYIRHWDQNERFLVVLNFGDVGLSAGLQA SDLPASASLPAKADLLLSTQPGREEGSPLELERLKLEPHEGLLLRFPYAA
>8X0W_2 Large neutral amino acids transporter small subunit 1 (chains B) VTLQRNITLLNGVAIIVGTIIGSGIFVTPTGVLKEAGSPGLALVVWAACGVFSIVGALCY AELGTTISKSGGDYAYMLEVYGSLPAFLKLWIELLIIRPSSQYIVALVFATYLLKPLFPT CPVPEEAAKLVACLCVLLLTAVNCYSVKAATRVQDAFAAAKLLALALIILLGFVQIGKGD VSNLDPNFSFEGTKLDVGNIVLALYSGLFAYGGWNYLNFVTEEMINPYRNLPLAIIISLP IVTLVYVLTNLAYFTTLSTEQMLSSEAVAVDFGNYHLGVMSWIIPVFVGLSCFGSVNGSL FTSSRLFFVGSREGHLPSILSMIHPQLLTPVPSLVFTCVMTLLYAFSKDIFSVINFFSFF NWLCVALAIIGMIWLRHRKPELERPIKVNLALPVFFILACLFLIAVSFWKTPVECGIGFT IILSGLPVYFFGVWWKNKPKWLLQGIFSTTVLCQKLMQVVPQET
| ID | Name | Formula | Copies |
|---|---|---|---|
| LEU | Leucine | C6 H13 N O2 | 1 |
Structural insights into the substrate transport mechanism of the amino acid transporter complex. Yang, H., Shi, T., Dong, J. et al. J Biol Chem (2025) 301:110569-110569. DOI 10.1016/j.jbc.2025.110569 · PubMed
Other PDB entries of the same protein (UniProt P08195 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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