Cryo-EM Structure of Human Transferrin Receptor 1 bound to DNA Aptamer. Determined by electron microscopy at 2.54 Å resolution. Released 17 Aug 2022.
Explore 7ZQS in 3D Show helices and sheets RCSB PDB PDBe
7ZQS contains 64 α-helices and 66 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 | 124-136 | 13 | |
| α-helix | 140-147 | 8 | |
| β-strand | 155 | 1 | 1 |
| α-helix | 160-175 | 16 | |
| β-strand | 180-182 | 3 | 2 |
| β-strand | 185-192 | 8 | 3 |
| α-helix | 197-198 | 2 | |
| β-strand | 199-203 | 5 | 4 |
| β-strand | 209-214 | 6 | 4 |
| β-strand | 220-221 | 2 | 5 |
| β-strand | 227-230 | 4 | 4 |
| β-strand | 232-234 | 3 | 6 |
| α-helix | 240-244 | 5 | |
| β-strand | 254-258 | 5 | 6 |
| α-helix | 264-273 | 10 | |
| β-strand | 278-282 | 5 | 6 |
| β-strand | 297 | 1 | 7 |
| β-strand | 299-300 | 2 | 5 |
| α-helix | 317-319 | 3 | |
| β-strand | 334-336 | 3 | 6 |
| α-helix | 339-346 | 8 | |
| β-strand | 349 | 1 | 8 |
| β-strand | 352 | 1 | 9 |
| β-strand | 364 | 1 | 9 |
| β-strand | 366 | 1 | 6 |
| β-strand | 367 | 1 | 8 |
| β-strand | 372-376 | 5 | 4 |
| β-strand | 380-387 | 8 | 3 |
| β-strand | 389-393 | 5 | 2 |
| β-strand | 402-408 | 7 | 2 |
| β-strand | 411 | 1 | 1 |
| α-helix | 416-420 | 5 | |
| α-helix | 421-435 | 15 | |
| α-helix | 436-440 | 5 | |
| β-strand | 447-453 | 7 | 2 |
| α-helix | 456-458 | 3 | |
| α-helix | 461-469 | 9 | |
| α-helix | 471-474 | 4 | |
| β-strand | 478-483 | 6 | 2 |
| β-strand | 488-489 | 2 | 2 |
| β-strand | 493-498 | 6 | 2 |
| α-helix | 500-502 | 3 | |
| α-helix | 503-510 | 8 | |
| β-strand | 514 | 1 | 10 |
| α-helix | 515 | 1 | |
| β-strand | 521 | 1 | 10 |
| α-helix | 528-531 | 4 | |
| α-helix | 532-535 | 4 | |
| α-helix | 541-542 | 2 | |
| α-helix | 543-547 | 5 | |
| β-strand | 552-558 | 7 | 2 |
| β-strand | 568 | 1 | 7 |
| α-helix | 573-579 | 7 | |
| α-helix | 583-602 | 20 | |
| α-helix | 611-613 | 3 | |
| α-helix | 614-625 | 12 | |
| α-helix | 626-628 | 3 | |
| α-helix | 629-634 | 6 | |
| α-helix | 640-662 | 23 | |
| α-helix | 668-683 | 16 | |
| β-strand | 686 | 1 | 11 |
| β-strand | 699 | 1 | 11 |
| α-helix | 709-721 | 13 | |
| α-helix | 728-750 | 23 | |
| α-helix | 753-755 | 3 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| DNA (30-mer) | A, C | DNA | 51 | unidentified | |
| Transferrin receptor protein 1 | B, D | protein | 760 | Homo sapiens | P02786 (AlphaFold model) |
>7ZQS_1 DNA (30-MER) (chains A, C) GCAGCAGCGTAAAGGGGGTGTTTGTGCGGTGTGGAGTGCGCGTGCTGCTGC
>7ZQS_2 Transferrin receptor protein 1 (chains B, D) MMDQARSAFSNLFGGEPLSYTRFSLARQVDGDNSHVEMKLAVDEEENADNNTKANVTKPK RCSGSICYGTIAVIVFFLIGFMIGYLGYCKGVEPKTECERLAGTESPVREEPGEDFPAAR RLYWDDLKRKLSEKLDSTDFTGTIKLLNENSYVPREAGSQKDENLALYVENQFREFKLSK VWRDQHFVKIQVKDSAQNSVIIVDKNGRLVYLVENPGGYVAYSKAATVTGKLVHANFGTK KDFEDLYTPVNGSIVIVRAGKITFAEKVANAESLNAIGVLIYMDQTKFPIVNAELSFFGH AHLGTGDPYTPGFPSFNHTQFPPSRSSGLPNIPVQTISRAAAEKLFGNMEGDCPSDWKTD STCRMVTSESKNVKLTVSNVLKEIKILNIFGVIKGFVEPDHYVVVGAQRDAWGPGAAKSG VGTALLLKLAQMFSDMVLKDGFQPSRSIIFASWSAGDFGSVGATEWLEGYLSSLHLKAFT YINLDKAVLGTSNFKVSASPLLYTLIEKTMQNVKHPVTGQFLYQDSNWASKVEKLTLDNA AFPFLAYSGIPAVSFCFCEDTDYPYLGTTMDTYKELIERIPELNKVARAAAEVAGQFVIK LTHDVELNLDYERYNSQLLSFVRDLNQYRADIKEMGLSLQWLYSARGDFFRATSRLTTDF GNAEKTDRFVMKKLNDRVMRVEYHFLSPYVSPKESPFRHVFWGSGSHTLPALLENLKLRK QNNGAFNETLFRNQLALATWTIQGAANALSGDVWDIDNEF
Discovery of a Transferrin Receptor 1-Binding Aptamer and Its Application in Cancer Cell Depletion for Adoptive T-Cell Therapy Manufacturing. Cheng, E.L., Cardle, I.I., Kacherovsky, N. et al. J Am Chem Soc (2022) 144:13851-13864. DOI 10.1021/jacs.2c05349 · PubMed
Other PDB entries of the same protein (UniProt P02786 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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