Crystal structure of human POT1 bound to telomeric single-stranded DNA (TTAGGGTTAG). Determined by X-ray diffraction at 1.73 Å resolution. Released 14 Dec 2004.
Explore 1XJV in 3D Show helices and sheets RCSB PDB PDBe
1XJV contains 15 α-helices and 14 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 | 11-13 | 3 | |
| α-helix | 14-16 | 3 | |
| β-strand | 21-37 | 17 | 1 |
| β-strand | 43-50 | 8 | 1 |
| β-strand | 56-63 | 8 | 1 |
| α-helix | 66-68 | 3 | |
| β-strand | 78-89 | 12 | 1 |
| β-strand | 92-106 | 15 | 1 |
| β-strand | 117 | 1 | 1 |
| α-helix | 127-143 | 17 | |
| α-helix | 153-155 | 3 | |
| β-strand | 161-173 | 13 | 2 |
| β-strand | 178-184 | 7 | 2 |
| α-helix | 192 | 1 | |
| β-strand | 193 | 1 | 2 |
| α-helix | 194 | 1 | |
| α-helix | 196-198 | 3 | |
| β-strand | 204-205 | 2 | 2 |
| α-helix | 207-213 | 7 | |
| α-helix | 214-216 | 3 | |
| β-strand | 218-223 | 6 | 2 |
| α-helix | 226-232 | 7 | |
| α-helix | 233-234 | 2 | |
| β-strand | 238-251 | 14 | 2 |
| β-strand | 257-265 | 9 | 2 |
| α-helix | 270-272 | 3 | |
| β-strand | 274-278 | 5 | 2 |
| α-helix | 279 | 1 | |
| α-helix | 283-297 | 15 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| hT10 d(TTAGGGTTAG) | B | DNA | 10 | ||
| Protection of telomeres 1 | A | protein | 294 | Homo sapiens | Q9NUX5 (AlphaFold model) |
>1XJV_1 hT10 d(TTAGGGTTAG) (chains B) TTAGGGTTAG
>1XJV_2 Protection of telomeres 1 (chains A) ATNYIYTPLNQLKGGTIVNVYGVVKFFKPPYLSKGTDYCSVVTIVDQTNVKLTCLLFSGN YEALPIIYKNGDIVRFHRLKIQVYKKETQGITSSGFASLTFEGTLGAPIIPRTSSKYFNF TTEDHKMVEALRVWASTHMSPSWTLLKLCDVQPMQYFDLTCQLLGKAEVDGASFLLKVWD GTRTPFPSWRVLIQDLVLEGDLSHIHRLQNLTIDILVYDNHVHVARSLKVGSFLRIYSLH TKLQSMNSENQTMLSLEFHLHGGTSYGRGIRVLPESNSDVDQLKKDLESANLTA
Structure of human POT1 bound to telomeric single-stranded DNA provides a model for chromosome end-protection. Lei, M., Podell, E.R., Cech, T.R. Nat Struct Mol Biol (2004) 11:1223-1229. DOI 10.1038/nsmb867 · PubMed
Other PDB entries of the same protein (UniProt Q9NUX5 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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