9GH7: Transferrin receptor protein 1

Complex of human TfR1 with a potent bicyclic peptide. Determined by X-ray diffraction at 2.08 Å resolution. Released 30 Apr 2025.

Method
X-ray diffraction
Resolution
2.08 Å
Organisms
Homo sapiens, synthetic construct
Chains
2
Atoms
5,290
Mol. weight
78.82 kDa
Ligands
A1ILE, CA
Released
30 Apr 2025

Explore 9GH7 in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

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.

Chain A: 31 helices, 28 β-strands

ElementResiduesLengthSheet
α-helix124-13714
α-helix140-1478
α-helix150-1523
β-strand15511
α-helix160-17516
β-strand180-193142
β-strand199-20463
β-strand209-21463
β-strand220-22124
α-helix223-2253
β-strand226-23053
β-strand232-23435
α-helix240-2445
β-strand254-25855
β-strand26016
β-strand26216
α-helix264-27310
β-strand278-28255
β-strand299-30024
α-helix317-3193
β-strand334-33635
α-helix339-3468
β-strand349-35025
α-helix355-3573
β-strand366-36725
β-strand371-37773
β-strand379-393152
β-strand398-408112
β-strand41111
α-helix416-4205
α-helix421-43818
β-strand446-45382
α-helix456-4583
α-helix461-47414
β-strand478-48362
β-strand48812
β-strand493-49862
α-helix500-5023
α-helix503-5108
β-strand51417
β-strand52117
α-helix528-5314
α-helix532-5354
α-helix541-5466
β-strand552-55872
α-helix562-5632
α-helix573-5797
α-helix583-60220
α-helix611-6133
α-helix614-62613
α-helix629-6346
α-helix640-66122
α-helix668-67811
α-helix683-6853
β-strand68618
β-strand69918
α-helix709-72113
α-helix728-74922
α-helix753-7553
Chain P: 1 helix, 0 β-strands
ElementResiduesLengthSheet
α-helix4-74

Molecules and chains

MoleculeChainsTypeLengthOrganismUniProt
Transferrin receptor protein 1Aprotein678Homo sapiensP02786 (AlphaFold model)
Bicyclic peptidePprotein15synthetic construct
Sequence of entity 1 (A), FASTA
>9GH7_1 Transferrin receptor protein 1 (chains A)
HHHHHHCKGVEPKTECERLAGTESPVREEPGEDFPAARRLYWDDLKRKLSEKLDSTDFTG
TIKLLNENSYVPREAGSQKDENLALYVENQFREFKLSKVWRDQHFVKIQVKDSAQNSVII
VDKNGRLVYLVENPGGYVAYSKAATVTGKLVHANFGTKKDFEDLYTPVNGSIVIVRAGKI
TFAEKVANAESLNAIGVLIYMDQTKFPIVNAELSFFGHAHLGTGDPYTPGFPSFNHTQFP
PSRSSGLPNIPVQTISRAAAEKLFGNMEGDCPSDWKTDSTCRMVTSESKNVKLTVSNVLK
EIKILNIFGVIKGFVEPDHYVVVGAQRDAWGPGAAKSGVGTALLLKLAQMFSDMVLKDGF
QPSRSIIFASWSAGDFGSVGATEWLEGYLSSLHLKAFTYINLDKAVLGTSNFKVSASPLL
YTLIEKTMQNVKHPVTGQFLYQDSNWASKVEKLTLDNAAFPFLAYSGIPAVSFCFCEDTD
YPYLGTTMDTYKELIERIPELNKVARAAAEVAGQFVIKLTHDVELNLDYERYNSQLLSFV
RDLNQYRADIKEMGLSLQWLYSARGDFFRATSRLTTDFGNAEKTDRFVMKKLNDRVMRVE
YHFLSPYVSPKESPFRHVFWGSGSHTLPALLENLKLRKQNNGAFNETLFRNQLALATWTI
QGAANALSGDVWDIDNEF
Sequence of entity 2 (P), FASTA
>9GH7_2 Bicyclic peptide (chains P)
ACPPDAHLGCISWCA

Ligands and cofactors

IDNameFormulaCopies
A1ILE1-(3,5-diethanoyl-1,3,5-triazinan-1-yl)ethanoneC9 H15 N3 O31
CACalcium ionCa1

Water and common crystallization additives (GOL) are not listed.

Primary citation

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:

Browse structure collections

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