3BQO: TRF1 TRFH domain and TIN2 peptide complex

Crystal Structure of TRF1 TRFH domain and TIN2 peptide complex. Determined by X-ray diffraction at 2.0 Å resolution. Released 19 Feb 2008.

Method
X-ray diffraction
Resolution
2.0 Å
Organism
Homo sapiens
Chains
2
Atoms
1,874
Mol. weight
26.69 kDa
Released
19 Feb 2008

Explore 3BQO in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

3BQO contains 10 α-helices and 2 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: 10 helices, 1 β-strand

ElementResiduesLengthSheet
α-helix63-9230
α-helix95-11016
α-helix117-13317
β-strand140-14121
α-helix150-1589
α-helix167-18620
α-helix190-20011
α-helix211-2199
α-helix226-2305
α-helix233-25119
α-helix255-26511
Chain B: 0 helices, 1 β-strand
ElementResiduesLengthSheet
β-strand264-26521

Molecules and chains

MoleculeChainsTypeLengthOrganismUniProt
Telomeric repeat-binding factor 1Aprotein211Homo sapiensP54274 (AlphaFold model)
TERF1-interacting nuclear factor 2Bprotein21Homo sapiensQ9BSI4 (AlphaFold model)
Sequence of entity 1 (A), FASTA
>3BQO_1 Telomeric repeat-binding factor 1 (chains A)
EEEEEDAGLVAEAEAVAAGWMLDFLCLSLCRAFRDGRSEDFRRTRNSAEAIIHGLSSLTA
CQLRTIYICQFLTRIAAGKTLDAQFENDERITPLESALMIWGSIEKEHDKLHEEIQNLIK
IQAIAVCMENGNFKEAEEVFERIFGDPNSHMPFKSKLLMIISQKDTFHSFFQHFSYNHMM
EKIKSYVNYVLSEKSSTFLMKAAAKVVESKR
Sequence of entity 2 (B), FASTA
>3BQO_2 TERF1-interacting nuclear factor 2 (chains B)
SHFNLAPLGRRRVQSQWASTR

Primary citation

A shared docking motif in TRF1 and TRF2 used for differential recruitment of telomeric proteins. Chen, Y., Yang, Y., van Overbeek, M. et al. Science (2008) 319:1092-1096. DOI 10.1126/science.1151804 · 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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