9HFG: Human TRF1 TRFH domain

Crystal structure of human TRF1 TRFH domain in complex with compound 14. Determined by X-ray diffraction at 2.02 Å resolution. Released 26 Nov 2025.

Method
X-ray diffraction
Resolution
2.02 Å
Organism
Homo sapiens
Chains
1
Atoms
1,677
Mol. weight
25.92 kDa
Ligands
A1A34
Released
26 Nov 2025

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

Secondary structure: helices and β-sheets

9HFG contains 11 α-helices and 0 β-strands across 1 chain. 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: 11 helices, 0 β-strands

ElementResiduesLengthSheet
α-helix64-9229
α-helix95-10814
α-helix109-1113
α-helix117-13317
α-helix150-1589
α-helix167-18620
α-helix190-20011
α-helix212-2198
α-helix226-2305
α-helix233-25119
α-helix255-26612

Molecules and chains

MoleculeChainsTypeLengthOrganismUniProt
Telomeric repeat-binding factor 1Aprotein224Homo sapiensP54274 (AlphaFold model)
Sequence of entity 1 (A), FASTA
>9HFG_1 Telomeric repeat-binding factor 1 (chains A)
SNAQVQVGAPEEEEEEEEDAGLVAEAEAVAAGWMLDFLCLSLCRAFRDGRSEDFRRTRNS
AEAIIHGLSSLTACQLRTIYICQFLTRIAAGKTLDAQFENDERITPLESALMIWGSIEKE
HDKLHEEIQNLIKIQAIAVCMENGNFKEAEEVFERIFGDPNSHMPFKSKLLMIISQKDTF
HSFFQHFSYNHMMEKIKSYVNYVLSEKSSTFLMKAAAKVVESKR

Ligands and cofactors

IDNameFormulaCopies
A1A342-methoxy-N-[(4-methylphenyl)methyl]acetamideC11 H15 N O21

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

Primary citation

Discovery of first-in-class inhibitors of the TRF1:TIN2 protein:protein interaction by fragment screening. Casale, G., Liu, M., Le Bihan, Y.V. et al. Sci Rep (2025) 15:40922-40922. DOI 10.1038/s41598-025-23858-3 · PubMed

Other PDB entries of the same protein (UniProt P54274 (AlphaFold model), which also has an AlphaFold model), best resolution first:

Browse structure collections

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