Solution Structure Of Human Trf2. Determined by solution NMR. Released 17 May 2005.
Explore 1VF9 in 3D Show helices and sheets RCSB PDB PDBe
1VF9 contains 4 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.
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 452-465 | 14 | |
| α-helix | 470-476 | 7 | |
| α-helix | 485-493 | 9 | |
| α-helix | 494-498 | 5 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Telomeric repeat binding factor 2 | A | protein | 64 | Homo sapiens | Q15554 (AlphaFold model) |
>1VF9_1 Telomeric repeat binding factor 2 (chains A) MEDSTTNITKKQKWTVEESEWVKAGVQKYGEGNWAAISKNYPFVNRTAVMIKDRWRTMKR LGMN
Comparison between TRF2 and TRF1 of their telomeric DNA-bound structures and DNA-binding activities. Hanaoka, S., Nagadoi, A., Nishimura, Y. Protein Sci (2005) 14:119-130. DOI 10.1110/ps.04983705 · PubMed
Other PDB entries of the same protein (UniProt Q15554 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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