Crystal structure of Pot1 (protection of telomere)- ssDNA complex. Determined by X-ray diffraction at 2.4 Å resolution. Released 25 Nov 2003.
Explore 1QZH in 3D Show helices and sheets RCSB PDB PDBe
1QZH contains 23 α-helices and 48 β-strands across 6 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 | 8-15 | 8 | |
| β-strand | 19-22 | 4 | 1 |
| β-strand | 25-28 | 4 | 1 |
| α-helix | 30-33 | 4 | |
| β-strand | 42-57 | 16 | 2 |
| β-strand | 65-72 | 8 | 2 |
| β-strand | 83-89 | 7 | 2 |
| β-strand | 104-114 | 11 | 2 |
| β-strand | 119-131 | 13 | 2 |
| α-helix | 144-147 | 4 | |
| β-strand | 151 | 1 | 2 |
| α-helix | 152-153 | 2 | |
| α-helix | 156-171 | 16 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 8-15 | 8 | |
| β-strand | 19-22 | 4 | 3 |
| β-strand | 25-28 | 4 | 3 |
| α-helix | 30-33 | 4 | |
| β-strand | 41-57 | 17 | 4 |
| β-strand | 65-72 | 8 | 4 |
| β-strand | 83-89 | 7 | 4 |
| β-strand | 104-114 | 11 | 4 |
| β-strand | 119-131 | 13 | 4 |
| β-strand | 151 | 1 | 4 |
| α-helix | 152-153 | 2 | |
| α-helix | 156-171 | 16 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 8-15 | 8 | |
| β-strand | 19-22 | 4 | 5 |
| β-strand | 25-28 | 4 | 5 |
| α-helix | 30-33 | 4 | |
| β-strand | 42-57 | 16 | 6 |
| β-strand | 65-72 | 8 | 6 |
| β-strand | 83-89 | 7 | 6 |
| β-strand | 104-114 | 11 | 6 |
| β-strand | 119-131 | 13 | 6 |
| β-strand | 151 | 1 | 6 |
| α-helix | 156-171 | 16 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 8-15 | 8 | |
| β-strand | 19-22 | 4 | 7 |
| β-strand | 25-28 | 4 | 7 |
| α-helix | 30-33 | 4 | |
| β-strand | 42-57 | 16 | 8 |
| β-strand | 65-72 | 8 | 8 |
| β-strand | 83-89 | 7 | 8 |
| β-strand | 104-115 | 12 | 8 |
| β-strand | 118-131 | 14 | 8 |
| α-helix | 144-147 | 4 | |
| β-strand | 151 | 1 | 8 |
| α-helix | 156-171 | 16 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 8-15 | 8 | |
| β-strand | 19-22 | 4 | 9 |
| β-strand | 25-28 | 4 | 9 |
| α-helix | 30-33 | 4 | |
| β-strand | 42-57 | 16 | 10 |
| β-strand | 65-72 | 8 | 10 |
| β-strand | 83-89 | 7 | 10 |
| β-strand | 104-114 | 11 | 10 |
| β-strand | 119-131 | 13 | 10 |
| β-strand | 151 | 1 | 10 |
| α-helix | 152-153 | 2 | |
| α-helix | 156-171 | 16 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| telomeric single-stranded DNA | G, H, I, J, K, L | DNA | 6 | ||
| Protection of telomeres protein 1 | A, B, C, D, E, F | protein | 187 | Schizosaccharomyces pombe | O13988 (AlphaFold model) |
>1QZH_1 telomeric single-stranded DNA (chains G, H, I, J, K, L) GGTTAC
>1QZH_2 Protection of telomeres protein 1 (chains A, B, C, D, E, F) GPGGEDVIDSLQLNELLNAGEYKIGELTFQSIRSSQELQKKNTIVNLFGIVKDFTPSRQS LHGTKDWVTTVYLWDPTCDTSSIGLQIHLFSKQGNDLPVIKQVGQPLLLHQITLRSYRDR TQGLSKDQFRYALWPDFSSNSKDTLCPQPMPRLMKTGDKEEQFALLLNKIWDEQTNKHKN GELLSTS
DNA self-recognition in the structure of Pot1 bound to telomeric single-stranded DNA. Lei, M., Podell, E.R., Baumann, P. et al. Nature (2003) 426:198-203. DOI 10.1038/nature02092 · PubMed
Other PDB entries of the same protein (UniProt O13988 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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