Overall structure of the LAT1-4F2hc bound with JX-078. Determined by electron microscopy at 2.9 Å resolution. Released 10 Mar 2021.
Explore 7DSL in 3D Show helices and sheets RCSB PDB PDBe
7DSL contains 47 α-helices and 24 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 | 179-205 | 27 | |
| α-helix | 209-214 | 6 | |
| α-helix | 219-221 | 3 | |
| β-strand | 225-228 | 4 | 1 |
| α-helix | 232-235 | 4 | |
| α-helix | 244-248 | 5 | |
| α-helix | 249-254 | 6 | |
| β-strand | 261-262 | 2 | 1 |
| α-helix | 263-264 | 2 | |
| β-strand | 266-268 | 3 | 2 |
| β-strand | 276-281 | 6 | 2 |
| α-helix | 288-299 | 12 | |
| β-strand | 306-308 | 3 | 1 |
| α-helix | 324-341 | 18 | |
| β-strand | 345-348 | 4 | 1 |
| α-helix | 351-353 | 3 | |
| α-helix | 357-369 | 13 | |
| β-strand | 376-380 | 5 | 1 |
| α-helix | 386-392 | 7 | |
| β-strand | 400-402 | 3 | 1 |
| α-helix | 413-427 | 15 | |
| β-strand | 432-434 | 3 | 3 |
| α-helix | 442-444 | 3 | |
| α-helix | 451-458 | 8 | |
| β-strand | 463-465 | 3 | 3 |
| β-strand | 466-468 | 3 | 1 |
| α-helix | 488-490 | 3 | |
| α-helix | 510-513 | 4 | |
| α-helix | 520-531 | 12 | |
| α-helix | 535-538 | 4 | |
| β-strand | 541-545 | 5 | 4 |
| β-strand | 551-557 | 7 | 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 | 599 | 1 | 4 |
| β-strand | 610-611 | 2 | 6 |
| β-strand | 616-617 | 2 | 5 |
| β-strand | 622-627 | 6 | 4 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 50 | 1 | 7 |
| α-helix | 52-63 | 12 | |
| α-helix | 67-70 | 4 | |
| α-helix | 72-79 | 8 | |
| α-helix | 82-109 | 28 | |
| α-helix | 118-123 | 6 | |
| α-helix | 126-135 | 10 | |
| α-helix | 136-140 | 5 | |
| α-helix | 141-157 | 17 | |
| α-helix | 158-160 | 3 | |
| α-helix | 165-167 | 3 | |
| α-helix | 168-188 | 21 | |
| α-helix | 190-220 | 31 | |
| α-helix | 240-252 | 13 | |
| β-strand | 267 | 1 | 7 |
| α-helix | 273-297 | 25 | |
| α-helix | 302-307 | 6 | |
| α-helix | 311-319 | 9 | |
| α-helix | 326-355 | 30 | |
| β-strand | 365-366 | 2 | 8 |
| α-helix | 374-385 | 12 | |
| α-helix | 386-389 | 4 | |
| α-helix | 401-420 | 20 | |
| α-helix | 431-432 | 2 | |
| α-helix | 435-453 | 19 | |
| α-helix | 455-466 | 12 | |
| α-helix | 469-472 | 4 | |
| α-helix | 473-477 | 5 | |
| α-helix | 483-500 | 18 | |
| β-strand | 503-504 | 2 | 8 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| 4F2 cell-surface antigen heavy chain | A | protein | 647 | Homo sapiens | P08195 (AlphaFold model) |
| Large neutral amino acids transporter small subunit 1 | B | protein | 527 | Homo sapiens | Q01650 (AlphaFold model) |
>7DSL_1 4F2 cell-surface antigen heavy chain (chains A) MAHHHHHHHHHHSGRELQPPEASIAVVSIPRQLPGSHSEAGVQGLSAGDDSETGSDCVTQ AGLQLLASSDPPALASKNAEVTVETGFHHVSQADIEFLTSIDPTASASGSAGITGTMSQD TEVDMKEVELNELEPEKQPMNAASGAAMSLAGAEKNGLVKIKVAEDEAEAAAAAKFTGLS KEELLKVAGSPGWVRTRWALLLLFWLGWLGMLAGAVVIIVRAPRCRELPAQKWWHTGALY RIGDLQAFQGHGAGNLAGLKGRLDYLSSLKVKGLVLGPIHKNQKDDVAQTDLLQIDPNFG SKEDFDSLLQSAKKKSIRVILDLTPNYRGENSWFSTQVDTVATKVKDALEFWLQAGVDGF QVRDIENLKDASSFLAEWQNITKGFSEDRLLIAGTNSSDLQQILSLLESNKDLLLTSSYL SDSGSTGEHTKSLVTQYLNATGNRWCSWSLSQARLLTSFLPAQLLRLYQLMLFTLPGTPV FSYGDEIGLDAAALPGQPMEAPVMLWDESSFPDIPGAVSANMTVKGQSEDPGSLLSLFRR LSDQRSKERSLLHGDFHAFSAGPGLFSYIRHWDQNERFLVVLNFGDVGLSAGLQASDLPA SASLPAKADLLLSTQPGREEGSPLELERLKLEPHEGLLLRFPYAALE
>7DSL_2 Large neutral amino acids transporter small subunit 1 (chains B) MADYKDDDDKSGPDEVDASGRAGAGPKRRALAAPAAEEKEEAREKMLAAKSADGSAPAGE GEGVTLQRNITLLNGVAIIVGTIIGSGIFVTPTGVLKEAGSPGLALVVWAACGVFSIVGA LCYAELGTTISKSGGDYAYMLEVYGSLPAFLKLWIELLIIRPSSQYIVALVFATYLLKPL FPTCPVPEEAAKLVACLCVLLLTAVNCYSVKAATRVQDAFAAAKLLALALIILLGFVQIG KGDVSNLDPNFSFEGTKLDVGNIVLALYSGLFAYGGWNYLNFVTEEMINPYRNLPLAIII SLPIVTLVYVLTNLAYFTTLSTEQMLSSEAVAVDFGNYHLGVMSWIIPVFVGLSCFGSVN GSLFTSSRLFFVGSREGHLPSILSMIHPQLLTPVPSLVFTCVMTLLYAFSKDIFSVINFF SFFNWLCVALAIIGMIWLRHRKPELERPIKVNLALPVFFILACLFLIAVSFWKTPVECGI GFTIILSGLPVYFFGVWWKNKPKWLLQGIFSTTVLCQKLMQVVPQET
| ID | Name | Formula | Copies |
|---|---|---|---|
| Y01 | Cholesterol hemisuccinate | C31 H50 O4 | 2 |
| HO0 | (2~{S})-2-azanyl-7-[(2-phenylphenyl)methoxy]-3,4-dihydro-1~{H}-naphthalene-2-ca… | C24 H23 N O3 | 1 |
| 3PH | 1,2-diacyl-glycerol-3-sn-phosphate | C39 H77 O8 P | 1 |
Mechanism of substrate transport and inhibition of the human LAT1-4F2hc amino acid transporter. Yan, R., Li, Y., Muller, J. et al. Cell Discov (2021) 7:16-16. DOI 10.1038/s41421-021-00247-4 · 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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