Complex of human TfR1 with a potent bicyclic peptide. Determined by X-ray diffraction at 2.08 Å resolution. Released 30 Apr 2025.
Explore 9GH7 in 3D Show helices and sheets RCSB PDB PDBe
9GH7 contains 32 α-helices and 28 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 | 124-137 | 14 | |
| α-helix | 140-147 | 8 | |
| α-helix | 150-152 | 3 | |
| β-strand | 155 | 1 | 1 |
| α-helix | 160-175 | 16 | |
| β-strand | 180-193 | 14 | 2 |
| β-strand | 199-204 | 6 | 3 |
| β-strand | 209-214 | 6 | 3 |
| β-strand | 220-221 | 2 | 4 |
| α-helix | 223-225 | 3 | |
| β-strand | 226-230 | 5 | 3 |
| β-strand | 232-234 | 3 | 5 |
| α-helix | 240-244 | 5 | |
| β-strand | 254-258 | 5 | 5 |
| β-strand | 260 | 1 | 6 |
| β-strand | 262 | 1 | 6 |
| α-helix | 264-273 | 10 | |
| β-strand | 278-282 | 5 | 5 |
| β-strand | 299-300 | 2 | 4 |
| α-helix | 317-319 | 3 | |
| β-strand | 334-336 | 3 | 5 |
| α-helix | 339-346 | 8 | |
| β-strand | 349-350 | 2 | 5 |
| α-helix | 355-357 | 3 | |
| β-strand | 366-367 | 2 | 5 |
| β-strand | 371-377 | 7 | 3 |
| β-strand | 379-393 | 15 | 2 |
| β-strand | 398-408 | 11 | 2 |
| β-strand | 411 | 1 | 1 |
| α-helix | 416-420 | 5 | |
| α-helix | 421-438 | 18 | |
| β-strand | 446-453 | 8 | 2 |
| α-helix | 456-458 | 3 | |
| α-helix | 461-474 | 14 | |
| β-strand | 478-483 | 6 | 2 |
| β-strand | 488 | 1 | 2 |
| β-strand | 493-498 | 6 | 2 |
| α-helix | 500-502 | 3 | |
| α-helix | 503-510 | 8 | |
| β-strand | 514 | 1 | 7 |
| β-strand | 521 | 1 | 7 |
| α-helix | 528-531 | 4 | |
| α-helix | 532-535 | 4 | |
| α-helix | 541-546 | 6 | |
| β-strand | 552-558 | 7 | 2 |
| α-helix | 562-563 | 2 | |
| α-helix | 573-579 | 7 | |
| α-helix | 583-602 | 20 | |
| α-helix | 611-613 | 3 | |
| α-helix | 614-626 | 13 | |
| α-helix | 629-634 | 6 | |
| α-helix | 640-661 | 22 | |
| α-helix | 668-678 | 11 | |
| α-helix | 683-685 | 3 | |
| β-strand | 686 | 1 | 8 |
| β-strand | 699 | 1 | 8 |
| α-helix | 709-721 | 13 | |
| α-helix | 728-749 | 22 | |
| α-helix | 753-755 | 3 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 4-7 | 4 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Transferrin receptor protein 1 | A | protein | 678 | Homo sapiens | P02786 (AlphaFold model) |
| Bicyclic peptide | P | protein | 15 | synthetic construct |
>9GH7_1 Transferrin receptor protein 1 (chains A) HHHHHHCKGVEPKTECERLAGTESPVREEPGEDFPAARRLYWDDLKRKLSEKLDSTDFTG TIKLLNENSYVPREAGSQKDENLALYVENQFREFKLSKVWRDQHFVKIQVKDSAQNSVII VDKNGRLVYLVENPGGYVAYSKAATVTGKLVHANFGTKKDFEDLYTPVNGSIVIVRAGKI TFAEKVANAESLNAIGVLIYMDQTKFPIVNAELSFFGHAHLGTGDPYTPGFPSFNHTQFP PSRSSGLPNIPVQTISRAAAEKLFGNMEGDCPSDWKTDSTCRMVTSESKNVKLTVSNVLK EIKILNIFGVIKGFVEPDHYVVVGAQRDAWGPGAAKSGVGTALLLKLAQMFSDMVLKDGF QPSRSIIFASWSAGDFGSVGATEWLEGYLSSLHLKAFTYINLDKAVLGTSNFKVSASPLL YTLIEKTMQNVKHPVTGQFLYQDSNWASKVEKLTLDNAAFPFLAYSGIPAVSFCFCEDTD YPYLGTTMDTYKELIERIPELNKVARAAAEVAGQFVIKLTHDVELNLDYERYNSQLLSFV RDLNQYRADIKEMGLSLQWLYSARGDFFRATSRLTTDFGNAEKTDRFVMKKLNDRVMRVE YHFLSPYVSPKESPFRHVFWGSGSHTLPALLENLKLRKQNNGAFNETLFRNQLALATWTI QGAANALSGDVWDIDNEF
>9GH7_2 Bicyclic peptide (chains P) ACPPDAHLGCISWCA
| ID | Name | Formula | Copies |
|---|---|---|---|
| A1ILE | 1-(3,5-diethanoyl-1,3,5-triazinan-1-yl)ethanone | C9 H15 N3 O3 | 1 |
| CA | Calcium ion | Ca | 1 |
Water and common crystallization additives (GOL) are not listed.
Conjugation to a transferrin receptor 1-binding Bicycle peptide enhances ASO and siRNA potency in skeletal and cardiac muscles. Ostergaard, M.E., Carrer, M., Anderson, B.A. et al. Nucleic Acids Res (2025) 53. DOI 10.1093/nar/gkaf270 · 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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