PIH1D1/phospho-Tel2 complex. Determined by X-ray diffraction at 2.45 Å resolution. Released 23 Apr 2014.
Explore 4PSI in 3D Show helices and sheets RCSB PDB PDBe
4PSI contains 8 α-helices and 16 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 | 40-43 | 4 | 1 |
| β-strand | 52-59 | 8 | 2 |
| β-strand | 64-72 | 9 | 2 |
| α-helix | 76-81 | 6 | |
| β-strand | 98-101 | 4 | 1 |
| β-strand | 102-103 | 2 | 2 |
| α-helix | 104-106 | 3 | |
| β-strand | 107-110 | 4 | 2 |
| β-strand | 116-125 | 10 | 2 |
| α-helix | 126-133 | 8 | |
| α-helix | 136-154 | 19 | |
| β-strand | 163-165 | 3 | 2 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| PIH1 domain-containing protein 1 | A, B | protein | 138 | Homo sapiens | Q9NWS0 (AlphaFold model) |
| Telomere length regulation protein TEL2 homolog | D, E | protein | 11 | Homo sapiens | Q9Y4R8 (AlphaFold model) |
>4PSI_1 PIH1 domain-containing protein 1 (chains A, B) AHSAALEVLFQGPGQPGFCIKTNSSEGKVFINICHSPSIPPPADVTEEELLQMLEEDQAG FRIPMSLGEPHAELDAKGQGCTAYDVAVNSDFYRRMQNSDFLRELVITIAREGLEDKYNL QLNPEWRMMKNRPFMGSI
>4PSI_2 Telomere length regulation protein TEL2 homolog (chains D, E) ALDSDDEFVPY
Phosphorylation-Dependent PIH1D1 Interactions Define Substrate Specificity of the R2TP Cochaperone Complex. Horejsi, Z., Stach, L., Flower, T.G. et al. Cell Rep (2014) 7:19-26. DOI 10.1016/j.celrep.2014.03.013 · PubMed
Other PDB entries of the same protein (UniProt Q9NWS0 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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