Structure of LAT1-CD98hc-Fab170 in complex with BCH, consensus map. Determined by electron microscopy at 3.68 Å resolution. Released 12 Feb 2025.
Explore 8KDG in 3D Show helices and sheets RCSB PDB PDBe
8KDG contains 67 α-helices and 69 β-strands across 4 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 | 208-215 | 8 | |
| α-helix | 218-221 | 4 | |
| β-strand | 224-227 | 4 | 1 |
| α-helix | 241-254 | 14 | |
| β-strand | 260-261 | 2 | 1 |
| β-strand | 265 | 1 | 2 |
| β-strand | 280 | 1 | 2 |
| α-helix | 282-284 | 3 | |
| α-helix | 287-300 | 14 | |
| β-strand | 305-307 | 3 | 1 |
| α-helix | 323-340 | 18 | |
| β-strand | 344-347 | 4 | 1 |
| α-helix | 350-352 | 3 | |
| α-helix | 356-370 | 15 | |
| β-strand | 375-379 | 5 | 1 |
| α-helix | 385-394 | 10 | |
| β-strand | 399-401 | 3 | 1 |
| α-helix | 415-426 | 12 | |
| α-helix | 441-443 | 3 | |
| α-helix | 450-457 | 8 | |
| β-strand | 465-467 | 3 | 1 |
| α-helix | 470-472 | 3 | |
| α-helix | 487-489 | 3 | |
| α-helix | 505-507 | 3 | |
| α-helix | 509-513 | 5 | |
| α-helix | 519-532 | 14 | |
| α-helix | 534-538 | 5 | |
| β-strand | 540-544 | 5 | 3 |
| β-strand | 545 | 1 | 4 |
| β-strand | 551-556 | 6 | 3 |
| β-strand | 562-567 | 6 | 3 |
| β-strand | 573-574 | 2 | 5 |
| β-strand | 581 | 1 | 4 |
| α-helix | 585-587 | 3 | |
| β-strand | 592-598 | 7 | 3 |
| β-strand | 608-610 | 3 | 3 |
| α-helix | 611-613 | 3 | |
| α-helix | 616-617 | 2 | |
| β-strand | 621-626 | 6 | 3 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 45-48 | 4 | |
| β-strand | 50 | 1 | 6 |
| 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 | 6 |
| 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 | 7 |
| β-strand | 367 | 1 | 8 |
| β-strand | 372 | 1 | 8 |
| α-helix | 374-385 | 12 | |
| α-helix | 386-389 | 4 | |
| α-helix | 393-396 | 4 | |
| α-helix | 397-421 | 25 | |
| 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 | 7 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 3-6 | 4 | 15 |
| β-strand | 9-12 | 4 | 16 |
| β-strand | 18-25 | 8 | 15 |
| α-helix | 29-31 | 3 | |
| β-strand | 34-39 | 6 | 16 |
| β-strand | 45-51 | 7 | 16 |
| β-strand | 58-60 | 3 | 16 |
| α-helix | 62-64 | 3 | |
| β-strand | 68-73 | 6 | 15 |
| β-strand | 78-83 | 6 | 15 |
| α-helix | 88-90 | 3 | |
| β-strand | 92-98 | 7 | 16 |
| β-strand | 109-110 | 2 | 16 |
| α-helix | 111-113 | 3 | |
| β-strand | 114-118 | 5 | 16 |
| α-helix | 122-123 | 2 | |
| β-strand | 124 | 1 | 17 |
| β-strand | 127-131 | 5 | 18 |
| α-helix | 137-139 | 3 | |
| β-strand | 142-152 | 11 | 18 |
| β-strand | 153 | 1 | 17 |
| β-strand | 158 | 1 | 19 |
| β-strand | 161 | 1 | 19 |
| β-strand | 170-178 | 9 | 18 |
| β-strand | 181-191 | 11 | 18 |
| α-helix | 195-197 | 3 | |
| β-strand | 201-206 | 6 | 19 |
| β-strand | 211-216 | 6 | 19 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 4-7 | 4 | 9 |
| β-strand | 10-14 | 5 | 10 |
| β-strand | 19-25 | 7 | 9 |
| β-strand | 30-31 | 2 | 11 |
| β-strand | 36-37 | 2 | 11 |
| β-strand | 39-44 | 6 | 10 |
| β-strand | 51-55 | 5 | 10 |
| β-strand | 59-60 | 2 | 10 |
| α-helix | 61 | 1 | |
| β-strand | 68-73 | 6 | 9 |
| β-strand | 76-81 | 6 | 9 |
| α-helix | 86-88 | 3 | |
| β-strand | 90-96 | 7 | 10 |
| β-strand | 99-100 | 2 | 5 |
| β-strand | 104 | 1 | 10 |
| β-strand | 108-113 | 6 | 10 |
| β-strand | 117 | 1 | 12 |
| α-helix | 118-119 | 2 | |
| β-strand | 120-124 | 5 | 13 |
| α-helix | 130-133 | 4 | |
| β-strand | 135-145 | 11 | 13 |
| β-strand | 146 | 1 | 12 |
| β-strand | 151-156 | 6 | 14 |
| β-strand | 159-161 | 3 | 14 |
| β-strand | 165-169 | 5 | 13 |
| α-helix | 170-173 | 4 | |
| β-strand | 179-188 | 10 | 13 |
| α-helix | 189-193 | 5 | |
| β-strand | 197-203 | 7 | 14 |
| α-helix | 210 | 1 | |
| β-strand | 211-216 | 6 | 14 |
| 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) |
| Fab170 light chain | L | protein | 220 | Mus musculus | |
| Fab170 heavy chain | H | protein | 230 | Mus musculus |
>8KDG_1 4F2 cell-surface antigen heavy chain (chains A) GSELQPPEASIAVVSIPRQLPGSHSEAGVQGLSAGDDSELGSHCVAQTGLELLASGDPLP SASQNAEMIETGSDCVTQAGLQLLASSDPPALASKNAEVTGTMSQDTEVDMKEVELNELE PEKQPMNAASGAAMSLAGAEKNGLVKIKVAEDEAEAAAAAKFTGLSKEELLKVAGSPGWV RTRWALLLLFWLGWLGMLAGAVVIIVRAPRCRELPAQKWWHTGALYRIGDLQAFQGHGAG NLAGLKGRLDYLSSLKVKGLVLGPIHKNQKDDVAQTDLLQIDPNFGSKEDFDSLLQSAKK KSIRVILDLTPNYRGENSWFSTQVDTVATKVKDALEFWLQAGVDGFQVRDIENLKDASSF LAEWQNITKGFSEDRLLIAGTNSSDLQQILSLLESNKDLLLTSSYLSDSGSTGEHTKSLV TQYLNATGNRWCSWSLSQARLLTSFLPAQLLRLYQLMLFTLPGTPVFSYGDEIGLDAAAL PGQPMEAPVMLWDESSFPDIPGAVSANMTVKGQSEDPGSLLSLFRRLSDQRSKERSLLHG DFHAFSAGPGLFSYIRHWDQNERFLVVLNFGDVGLSAGLQASDLPASASLPAKADLLLST QPGREEGSPLELERLKLEPHEGLLLRFPYAA
>8KDG_2 Large neutral amino acids transporter small subunit 1 (chains B) MAGAGPKRRALAAPAAEEKEEAREKMLAAKSADGSAPAGEGEGVTLQRNITLLNGVAIIV GTIIGSGIFVTPTGVLKEAGSPGLALVVWAACGVFSIVGALCYAELGTTISKSGGDYAYM LEVYGSLPAFLKLWIELLIIRPSSQYIVALVFATYLLKPLFPTCPVPEEAAKLVACLCVL LLTAVNCYSVKAATRVQDAFAAAKLLALALIILLGFVQIGKGDVSNLDPNFSFEGTKLDV GNIVLALYSGLFAYGGWNYLNFVTEEMINPYRNLPLAIIISLPIVTLVYVLTNLAYFTTL STEQMLSSEAVAVDFGNYHLGVMSWIIPVFVGLSCFGSVNGSLFTSSRLFFVGSREGHLP SILSMIHPQLLTPVPSLVFTCVMTLLYAFSKDIFSVINFFSFFNWLCVALAIIGMIWLRH RKPELERPIKVNLALPVFFILACLFLIAVSFWKTPVECGIGFTIILSGLPVYFFGVWWKN KPKWLLQGIFSTTVLCQKLMQVVPQETDYKDDDDK
>8KDG_3 Fab170 light chain (chains L) DIVLTQSPSSLAMSVGQKVTMNCKSSQSLLNNNNQKNYLAWYQQKPGQSPKLLVYFTSTR ESGVPDRFIGSGSGTDFTLTISSVQAEDLALYYCQQHYTIPPTFGGGTKLEIKRADAAPT VSIFPPSSEQLTSGGASVVCFLNNFYPKDINVKWKIDGSERQNGVLNSWTDQDSKDSTYS MSSTLTLTKDEYERHNSYTCEATHKTSTSPIVKSFNRNEC
>8KDG_4 Fab170 heavy chain (chains H) EVQLQQSGAELVKPGASVNLSCKASGYTFTNYWMHWVRLRPGQGLEWIGEIDPSDSYSYY SQNFKGKATLTVDQSSNTAYLQLTSLTSEDSAVYYCARGRQTYYPWFPYWGQGTLVTVSA AKTTPPSDYPLAPGSAAQTNSMVTLGCLVKGYFPEPVTVTWNSGSLSSGVHTFPAVLQSD LYTLSSSVTVPSSTWPSETVTCNVAHPASSTKVDKKIVPRDCGCKPCICT
| ID | Name | Formula | Copies |
|---|---|---|---|
| NAG | 2-acetamido-2-deoxy-beta-D-glucopyranose | C8 H15 N O6 | 4 |
| VU0 | (1~{S},2~{R},4~{R})-2-azanylbicyclo[2.2.1]heptane-2-carboxylic acid | C8 H13 N O2 | 1 |
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:
MolViewer shows 8KDG directly in your browser with nothing to install. Switch between cartoon, ball-and-stick, spacefill and surface views, color by chain, secondary structure or B-factor, measure distances, angles and dihedrals, and share or embed the view.