Structure of the human POT1-TPP1 telomeric complex. Determined by X-ray diffraction at 2.1 Å resolution. Released 12 Apr 2017.
Explore 5UN7 in 3D Show helices and sheets RCSB PDB PDBe
5UN7 contains 21 α-helices and 26 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 |
|---|---|---|---|
| β-strand | 335-337 | 3 | 1 |
| α-helix | 344 | 1 | |
| β-strand | 345 | 1 | 1 |
| α-helix | 348-352 | 5 | |
| α-helix | 355 | 1 | |
| β-strand | 359-370 | 12 | 1 |
| α-helix | 374-376 | 3 | |
| β-strand | 378-381 | 4 | 1 |
| β-strand | 388-390 | 3 | 1 |
| α-helix | 391-393 | 3 | |
| α-helix | 394-403 | 10 | |
| β-strand | 406 | 1 | 2 |
| α-helix | 413-415 | 3 | |
| β-strand | 419-424 | 6 | 3 |
| β-strand | 427 | 1 | 4 |
| β-strand | 433 | 1 | 2 |
| β-strand | 434-439 | 6 | 3 |
| β-strand | 441 | 1 | 5 |
| β-strand | 444 | 1 | 5 |
| α-helix | 448-450 | 3 | |
| β-strand | 452-456 | 5 | 3 |
| α-helix | 460-469 | 10 | |
| β-strand | 472-475 | 4 | 3 |
| β-strand | 476-478 | 3 | 6 |
| β-strand | 483-485 | 3 | 6 |
| β-strand | 493-495 | 3 | 3 |
| β-strand | 498-500 | 3 | 3 |
| β-strand | 502 | 1 | 7 |
| α-helix | 512-517 | 6 | |
| α-helix | 526-532 | 7 | |
| β-strand | 537 | 1 | 7 |
| β-strand | 539-549 | 11 | 1 |
| β-strand | 554-561 | 8 | 1 |
| α-helix | 570-573 | 4 | |
| α-helix | 577-590 | 14 | |
| α-helix | 597-599 | 3 | |
| α-helix | 601-602 | 2 | |
| β-strand | 603-613 | 11 | 1 |
| β-strand | 618-625 | 8 | 1 |
| β-strand | 627-629 | 3 | 1 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 267-278 | 12 | |
| β-strand | 282 | 1 | 4 |
| α-helix | 287-289 | 3 | |
| α-helix | 292-299 | 8 | |
| α-helix | 304-306 | 3 | |
| α-helix | 310-313 | 4 | |
| α-helix | 317-324 | 8 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Protection of telomeres protein 1 | A | protein | 308 | Homo sapiens | Q9NUX5 (AlphaFold model) |
| Adrenocortical dysplasia protein homolog | B | protein | 86 | Homo sapiens | Q96AP0 (AlphaFold model) |
>5UN7_1 Protection of telomeres protein 1 (chains A) SNAQQLSATILTDHQYLERTPLCAILKQKAPQQYRIRAKLRSYKPRRLFQSVKLHCPKCH LLQEVPHEGDLDIIFQDGATKTPDVKLQNTSLYDSKIWTTKNQKGRKVAVHFVKNNGILP LSNECLLLIEGGTLSEICKLSNKFNSVIPVRSGHEDLELLDLSAPFLIQGTIHHYGCKQC SSLRSIQNLNSLVDKTSWIPSSVAEALGIVPLQYVFVMTFTLDDGTGVLEAYLMDSDKFF QIPASEVLMDDDLQKSVDMIMDMFCPPGIKIDAYPWLECFIKSYNVTNGTDNQICYQIFD TTVAEDVI
>5UN7_2 Adrenocortical dysplasia protein homolog (chains B) SNASQLLDEMREDQEHQGALVCLAESCLTLEGPCTAPPVTHWAASRCKATGEAVYTVPSS MLCISENDQLILSSLGPCQRTQGPEL
| ID | Name | Formula | Copies |
|---|---|---|---|
| ZN | Zinc ion | Zn | 1 |
Water and common crystallization additives (K) are not listed.
Structural and functional analysis of the human POT1-TPP1 telomeric complex. Rice, C., Shastrula, P.K., Kossenkov, A.V. et al. Nat Commun (2017) 8:14928-14928. DOI 10.1038/ncomms14928 · 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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