Structure of LAT1-CD98hc in complex with BCH, focused on TMD. Determined by electron microscopy at 3.78 Å resolution. Released 12 Feb 2025.
Explore 8KDH in 3D Show helices and sheets RCSB PDB PDBe
8KDH contains 33 α-helices and 6 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 | 166-173 | 8 | |
| α-helix | 176-206 | 31 | |
| α-helix | 208-212 | 5 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 45-48 | 4 | |
| β-strand | 50 | 1 | 1 |
| α-helix | 52-64 | 13 | |
| α-helix | 67-70 | 4 | |
| α-helix | 72-79 | 8 | |
| α-helix | 82-110 | 29 | |
| α-helix | 115-124 | 10 | |
| 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 | 190-221 | 32 | |
| α-helix | 240-254 | 15 | |
| α-helix | 260-262 | 3 | |
| β-strand | 267 | 1 | 1 |
| α-helix | 270-299 | 30 | |
| α-helix | 302-307 | 6 | |
| α-helix | 311-320 | 10 | |
| α-helix | 321-323 | 3 | |
| α-helix | 326-355 | 30 | |
| α-helix | 361-364 | 4 | |
| β-strand | 366 | 1 | 2 |
| β-strand | 367 | 1 | 3 |
| β-strand | 372 | 1 | 3 |
| α-helix | 374-385 | 12 | |
| α-helix | 386-389 | 4 | |
| α-helix | 393-395 | 3 | |
| α-helix | 396-421 | 26 | |
| α-helix | 434-453 | 20 | |
| α-helix | 455-466 | 12 | |
| α-helix | 468-472 | 5 | |
| α-helix | 473-477 | 5 | |
| α-helix | 483-500 | 18 | |
| β-strand | 503 | 1 | 2 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| 4F2 cell-surface antigen heavy chain | A | protein | 631 | Homo sapiens | P08195 (AlphaFold model) |
| Large neutral amino acids transporter small subunit 1 | B | protein | 515 | Homo sapiens | Q01650 (AlphaFold model) |
>8KDH_1 4F2 cell-surface antigen heavy chain (chains A) GSELQPPEASIAVVSIPRQLPGSHSEAGVQGLSAGDDSELGSHCVAQTGLELLASGDPLP SASQNAEMIETGSDCVTQAGLQLLASSDPPALASKNAEVTGTMSQDTEVDMKEVELNELE PEKQPMNAASGAAMSLAGAEKNGLVKIKVAEDEAEAAAAAKFTGLSKEELLKVAGSPGWV RTRWALLLLFWLGWLGMLAGAVVIIVRAPRCRELPAQKWWHTGALYRIGDLQAFQGHGAG NLAGLKGRLDYLSSLKVKGLVLGPIHKNQKDDVAQTDLLQIDPNFGSKEDFDSLLQSAKK KSIRVILDLTPNYRGENSWFSTQVDTVATKVKDALEFWLQAGVDGFQVRDIENLKDASSF LAEWQNITKGFSEDRLLIAGTNSSDLQQILSLLESNKDLLLTSSYLSDSGSTGEHTKSLV TQYLNATGNRWCSWSLSQARLLTSFLPAQLLRLYQLMLFTLPGTPVFSYGDEIGLDAAAL PGQPMEAPVMLWDESSFPDIPGAVSANMTVKGQSEDPGSLLSLFRRLSDQRSKERSLLHG DFHAFSAGPGLFSYIRHWDQNERFLVVLNFGDVGLSAGLQASDLPASASLPAKADLLLST QPGREEGSPLELERLKLEPHEGLLLRFPYAA
>8KDH_2 Large neutral amino acids transporter small subunit 1 (chains B) MAGAGPKRRALAAPAAEEKEEAREKMLAAKSADGSAPAGEGEGVTLQRNITLLNGVAIIV GTIIGSGIFVTPTGVLKEAGSPGLALVVWAACGVFSIVGALCYAELGTTISKSGGDYAYM LEVYGSLPAFLKLWIELLIIRPSSQYIVALVFATYLLKPLFPTCPVPEEAAKLVACLCVL LLTAVNCYSVKAATRVQDAFAAAKLLALALIILLGFVQIGKGDVSNLDPNFSFEGTKLDV GNIVLALYSGLFAYGGWNYLNFVTEEMINPYRNLPLAIIISLPIVTLVYVLTNLAYFTTL STEQMLSSEAVAVDFGNYHLGVMSWIIPVFVGLSCFGSVNGSLFTSSRLFFVGSREGHLP SILSMIHPQLLTPVPSLVFTCVMTLLYAFSKDIFSVINFFSFFNWLCVALAIIGMIWLRH RKPELERPIKVNLALPVFFILACLFLIAVSFWKTPVECGIGFTIILSGLPVYFFGVWWKN KPKWLLQGIFSTTVLCQKLMQVVPQETDYKDDDDK
| ID | Name | Formula | Copies |
|---|---|---|---|
| VU0 | (1~{S},2~{R},4~{R})-2-azanylbicyclo[2.2.1]heptane-2-carboxylic acid | C8 H13 N O2 | 1 |
| LBN | 1-palmitoyl-2-oleoyl-sn-glycero-3-phosphocholine | C42 H82 N O8 P | 1 |
| CLR | Cholesterol | C27 H46 O | 2 |
Structural basis of anticancer drug recognition and amino acid transport by LAT1. Lee, Y., Jin, C., Ohgaki, R. et al. Nat Commun (2025) 16:1635-1635. DOI 10.1038/s41467-025-56903-w · 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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