Crystal Structure of TRF1 TRFH domain and TIN2 peptide complex. Determined by X-ray diffraction at 2.0 Å resolution. Released 19 Feb 2008.
Explore 3BQO in 3D Show helices and sheets RCSB PDB PDBe
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.
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 63-92 | 30 | |
| α-helix | 95-110 | 16 | |
| α-helix | 117-133 | 17 | |
| β-strand | 140-141 | 2 | 1 |
| α-helix | 150-158 | 9 | |
| α-helix | 167-186 | 20 | |
| α-helix | 190-200 | 11 | |
| α-helix | 211-219 | 9 | |
| α-helix | 226-230 | 5 | |
| α-helix | 233-251 | 19 | |
| α-helix | 255-265 | 11 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 264-265 | 2 | 1 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Telomeric repeat-binding factor 1 | A | protein | 211 | Homo sapiens | P54274 (AlphaFold model) |
| TERF1-interacting nuclear factor 2 | B | protein | 21 | Homo sapiens | Q9BSI4 (AlphaFold model) |
>3BQO_1 Telomeric repeat-binding factor 1 (chains A) EEEEEDAGLVAEAEAVAAGWMLDFLCLSLCRAFRDGRSEDFRRTRNSAEAIIHGLSSLTA CQLRTIYICQFLTRIAAGKTLDAQFENDERITPLESALMIWGSIEKEHDKLHEEIQNLIK IQAIAVCMENGNFKEAEEVFERIFGDPNSHMPFKSKLLMIISQKDTFHSFFQHFSYNHMM EKIKSYVNYVLSEKSSTFLMKAAAKVVESKR
>3BQO_2 TERF1-interacting nuclear factor 2 (chains B) SHFNLAPLGRRRVQSQWASTR
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:
MolViewer shows 3BQO directly in your browser with nothing to install. Switch between cartoon, ball-and-stick, spacefill and surface views, color by chain, secondary structure or B-factor, measure distances, angles and dihedrals, and share or embed the view.