Overall structure of the LAT1-4F2hc bound with JPH203. Determined by electron microscopy at 3.3 Å resolution. Released 17 Jul 2024.
Explore 8XPU in 3D Show helices and sheets RCSB PDB PDBe
8XPU contains 45 α-helices and 25 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 | 180-206 | 27 | |
| α-helix | 209-211 | 3 | |
| α-helix | 219-221 | 3 | |
| β-strand | 225-228 | 4 | 1 |
| α-helix | 231-235 | 5 | |
| α-helix | 243-255 | 13 | |
| β-strand | 260-262 | 3 | 1 |
| α-helix | 263-264 | 2 | |
| β-strand | 266 | 1 | 2 |
| β-strand | 281 | 1 | 2 |
| α-helix | 288-300 | 13 | |
| β-strand | 305-306 | 2 | 1 |
| β-strand | 307-308 | 2 | 3 |
| α-helix | 325-341 | 17 | |
| β-strand | 346-348 | 3 | 3 |
| α-helix | 357-371 | 15 | |
| β-strand | 377-381 | 5 | 3 |
| α-helix | 386-392 | 7 | |
| β-strand | 400-403 | 4 | 3 |
| α-helix | 414-427 | 14 | |
| β-strand | 432-434 | 3 | 4 |
| α-helix | 442-445 | 4 | |
| α-helix | 451-458 | 8 | |
| β-strand | 463-465 | 3 | 4 |
| β-strand | 466-468 | 3 | 1 |
| α-helix | 488-490 | 3 | |
| α-helix | 510-514 | 5 | |
| α-helix | 520-533 | 14 | |
| α-helix | 535-539 | 5 | |
| β-strand | 541-544 | 4 | 5 |
| β-strand | 551-557 | 7 | 5 |
| β-strand | 563-569 | 7 | 5 |
| β-strand | 575-576 | 2 | 6 |
| α-helix | 586-588 | 3 | |
| β-strand | 593-594 | 2 | 7 |
| β-strand | 599 | 1 | 5 |
| β-strand | 610-611 | 2 | 7 |
| β-strand | 616-617 | 2 | 6 |
| β-strand | 621-627 | 7 | 5 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 50 | 1 | 8 |
| α-helix | 52-63 | 12 | |
| α-helix | 73-79 | 7 | |
| 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 | 191-219 | 29 | |
| α-helix | 244-248 | 5 | |
| α-helix | 256-258 | 3 | |
| α-helix | 260-262 | 3 | |
| β-strand | 267 | 1 | 8 |
| α-helix | 270-299 | 30 | |
| α-helix | 302-306 | 5 | |
| α-helix | 314-318 | 5 | |
| α-helix | 326-353 | 28 | |
| α-helix | 354-356 | 3 | |
| β-strand | 367 | 1 | 9 |
| β-strand | 372 | 1 | 9 |
| α-helix | 374-385 | 12 | |
| α-helix | 386-389 | 4 | |
| α-helix | 401-421 | 21 | |
| α-helix | 435-453 | 19 | |
| α-helix | 455-466 | 12 | |
| α-helix | 469-473 | 5 | |
| α-helix | 486-500 | 15 | |
| α-helix | 504-506 | 3 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Isoform 5 of Amino acid transporter heavy chain SLC3A2 | A | protein | 647 | Homo sapiens | P08195 (AlphaFold model) |
| Large neutral amino acids transporter small subunit 1 | B | protein | 527 | Homo sapiens | Q01650 (AlphaFold model) |
>8XPU_1 Isoform 5 of Amino acid transporter heavy chain SLC3A2 (chains A) MAHHHHHHHHHHSGRELQPPEASIAVVSIPRQLPGSHSEAGVQGLSAGDDSETGSDCVTQ AGLQLLASSDPPALASKNAEVTVETGFHHVSQADIEFLTSIDPTASASGSAGITGTMSQD TEVDMKEVELNELEPEKQPMNAASGAAMSLAGAEKNGLVKIKVAEDEAEAAAAAKFTGLS KEELLKVAGSPGWVRTRWALLLLFWLGWLGMLAGAVVIIVRAPRCRELPAQKWWHTGALY RIGDLQAFQGHGAGNLAGLKGRLDYLSSLKVKGLVLGPIHKNQKDDVAQTDLLQIDPNFG SKEDFDSLLQSAKKKSIRVILDLTPNYRGENSWFSTQVDTVATKVKDALEFWLQAGVDGF QVRDIENLKDASSFLAEWQNITKGFSEDRLLIAGTNSSDLQQILSLLESNKDLLLTSSYL SDSGSTGEHTKSLVTQYLNATGNRWCSWSLSQARLLTSFLPAQLLRLYQLMLFTLPGTPV FSYGDEIGLDAAALPGQPMEAPVMLWDESSFPDIPGAVSANMTVKGQSEDPGSLLSLFRR LSDQRSKERSLLHGDFHAFSAGPGLFSYIRHWDQNERFLVVLNFGDVGLSAGLQASDLPA SASLPAKADLLLSTQPGREEGSPLELERLKLEPHEGLLLRFPYAALE
>8XPU_2 Large neutral amino acids transporter small subunit 1 (chains B) MADYKDDDDKSGPDEVDASGRAGAGPKRRALAAPAAEEKEEAREKMLAAKSADGSAPAGE GEGVTLQRNITLLNGVAIIVGTIIGSGIFVTPTGVLKEAGSPGLALVVWAACGVFSIVGA LCYAELGTTISKSGGDYAYMLEVYGSLPAFLKLWIELLIIRPSSQYIVALVFATYLLKPL FPTCPVPEEAAKLVACLCVLLLTAVNCYSVKAATRVQDAFAAAKLLALALIILLGFVQIG KGDVSNLDPNFSFEGTKLDVGNIVLALYSGLFAYGGWNYLNFVTEEMINPYRNLPLAIII SLPIVTLVYVLTNLAYFTTLSTEQMLSSEAVAVDFGNYHLGVMSWIIPVFVGLSCFGSVN GSLFTSSRLFFVGSREGHLPSILSMIHPQLLTPVPSLVFTCVMTLLYAFSKDIFSVINFF SFFNWLCVALAIIGMIWLRHRKPELERPIKVNLALPVFFILACLFLIAVSFWKTPVECGI GFTIILSGLPVYFFGVWWKNKPKWLLQGIFSTTVLCQKLMQVVPQET
| ID | Name | Formula | Copies |
|---|---|---|---|
| VRW | Nanvuranlat | C23 H19 Cl2 N3 O4 | 1 |
Structural basis for the inhibition mechanism of LAT1-4F2hc complex by JPH203. Hu, Z., Yan, R. Cell Discov (2024) 10:73-73. DOI 10.1038/s41421-024-00697-6 · 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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