Tetratricopeptide repeats of protein phosphatase 5. Determined by X-ray diffraction at 2.45 Å resolution. Released 29 Apr 1998.
Explore 1A17 in 3D Show helices and sheets RCSB PDB PDBe
1A17 contains 7 α-helices and 0 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 | 22-40 | 19 | |
| α-helix | 44-57 | 14 | |
| α-helix | 62-74 | 13 | |
| α-helix | 78-91 | 14 | |
| α-helix | 96-108 | 13 | |
| α-helix | 112-125 | 14 | |
| α-helix | 130-164 | 35 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Serine/threonine protein phosphatase 5 | A | protein | 166 | Homo sapiens | P53041 (AlphaFold model) |
>1A17_1 SERINE/THREONINE PROTEIN PHOSPHATASE 5 (chains A) RDEPPADGALKRAEELKTQANDYFKAKDYENAIKFYSQAIELNPSNAIYYGNRSLAYLRT ECYGYALGDATRAIELDKKYIKGYYRRAASNMALGKFRAALRDYETVVKVKPHDKDAKMK YQECNKIVKQKAFERAIAGDEHKRSVVDSLDIESMTIEDEYSGPKL
The structure of the tetratricopeptide repeats of protein phosphatase 5: implications for TPR-mediated protein-protein interactions. Das, A.K., Cohen, P.W., Barford, D. EMBO J (1998) 17:1192-1199. DOI 10.1093/emboj/17.5.1192 · PubMed
Other PDB entries of the same protein (UniProt P53041 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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