Structural Basis for Telomere Length Regulation by the Shelterin Bridge. Determined by X-ray diffraction at 2.5 Å resolution. Released 20 Dec 2017.
Explore 5WE2 in 3D Show helices and sheets RCSB PDB PDBe
5WE2 contains 28 α-helices and 0 β-strands across 4 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 | 2-18 | 17 | |
| α-helix | 28-43 | 16 | |
| α-helix | 45-49 | 5 | |
| α-helix | 51-53 | 3 | |
| α-helix | 54-64 | 11 | |
| α-helix | 93-114 | 22 | |
| α-helix | 130-157 | 28 | |
| α-helix | 164-174 | 11 | |
| α-helix | 176-178 | 3 | |
| α-helix | 179-188 | 10 | |
| α-helix | 193-206 | 14 | |
| α-helix | 209-230 | 22 | |
| α-helix | 238-244 | 7 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 480-483 | 4 | |
| α-helix | 490-504 | 15 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 2-18 | 17 | |
| α-helix | 28-43 | 16 | |
| α-helix | 45-49 | 5 | |
| α-helix | 54-64 | 11 | |
| α-helix | 93-114 | 22 | |
| α-helix | 130-157 | 28 | |
| α-helix | 164-174 | 11 | |
| α-helix | 182-189 | 8 | |
| α-helix | 193-206 | 14 | |
| α-helix | 209-230 | 22 | |
| α-helix | 238-240 | 3 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 482-484 | 3 | |
| α-helix | 490-506 | 17 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Protection of telomeres protein poz1 | A, C | protein | 249 | Schizosaccharomyces pombe (strain 972 / ATCC 24843) | O13852 (AlphaFold model) |
| Protection of telomeres protein tpz1 | B, D | protein | 33 | Schizosaccharomyces pombe (strain 972 / ATCC 24843) | O14246 (AlphaFold model) |
| DNA-binding protein rap1 | F | protein | 30 | Schizosaccharomyces pombe (strain 972 / ATCC 24843) | Q96TL7 (AlphaFold model) |
>5WE2_1 Protection of telomeres protein poz1 (chains A, C) SNEKIRSQSVLNTLETFFIKENHYDMQREESSIVNACLRYLGYSKSMCHEKMPIFMDIAF IEYCFNLSLDPSSFQNLPITQTQPDSQQILWEYSLISNALERLENIELERQNCMREDGLV KYTNELLLNKETLNNEALKLYSCAKAGICRWMAFHFLEQEPIDHINFTKFLQDWGSHNEK EMEALQRLSKHKIRKRLIYVSQHKKKMPWSKFNSVLSRYIQCTKLQLEVFCDYDFKQREI VKMLTSNIN
>5WE2_2 Protection of telomeres protein tpz1 (chains B, D) SEACEMCRLGLPHGSFFELLRDWKKIEEFRNKS
>5WE2_3 DNA-binding protein rap1 (chains F) SDNIFVKPGEDLEIPLLSDYSDSENISEKS
| ID | Name | Formula | Copies |
|---|---|---|---|
| ZN | Zinc ion | Zn | 2 |
Structural Basis for Shelterin Bridge Assembly. Kim, J.K., Liu, J., Hu, X. et al. Mol Cell (2017) 68:698-714.e5. DOI 10.1016/j.molcel.2017.10.032 · PubMed
Other PDB entries of the same protein (UniProt O13852 (AlphaFold model), which also has an AlphaFold model), best resolution first:
MolViewer shows 5WE2 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.