Structure of human PTPA. Determined by X-ray diffraction at 1.5 Å resolution. Released 11 Jul 2006.
Explore 2IXM in 3D Show helices and sheets RCSB PDB PDBe
2IXM contains 25 α-helices and 7 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 |
|---|---|---|---|
| β-strand | 27-28 | 2 | 1 |
| α-helix | 34-40 | 7 | |
| β-strand | 42 | 1 | 2 |
| α-helix | 43-58 | 16 | |
| α-helix | 72-89 | 18 | |
| α-helix | 92-95 | 4 | |
| α-helix | 104-121 | 18 | |
| α-helix | 126-131 | 6 | |
| α-helix | 132-140 | 9 | |
| β-strand | 145 | 1 | 3 |
| β-strand | 150-151 | 2 | 3 |
| α-helix | 153-168 | 16 | |
| α-helix | 174-176 | 3 | |
| α-helix | 177-179 | 3 | |
| α-helix | 180-185 | 6 | |
| α-helix | 186-198 | 13 | |
| α-helix | 201 | 1 | |
| β-strand | 202-203 | 2 | 3 |
| α-helix | 208-210 | 3 | |
| α-helix | 218-226 | 9 | |
| α-helix | 235-239 | 5 | |
| α-helix | 241-247 | 7 | |
| α-helix | 248-250 | 3 | |
| α-helix | 252-263 | 12 | |
| α-helix | 268-271 | 4 | |
| α-helix | 273-278 | 6 | |
| α-helix | 284-295 | 12 | |
| α-helix | 296-300 | 5 | |
| α-helix | 303-306 | 4 | |
| β-strand | 310-311 | 2 | 1 |
| β-strand | 319 | 1 | 2 |
| α-helix | 320-321 | 2 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Serine/threonine-protein phosphatase 2A regulatory subunit B' | A | protein | 303 | HOMO SAPIENS | Q15257 (AlphaFold model) |
>2IXM_1 SERINE/THREONINE-PROTEIN PHOSPHATASE 2A REGULATORY SUBUNIT B' (chains A) TQNFIIPKKEIHTVPDMGKWKRSQAYADYIGFILTLNEGVKGKKLTFEYRVSEAIEKLLA LLNTLDRWIDETPPVDQPSRFGNKAYRTWYAKLDEEAENLVATVVPTHLAAAVPEVAVYL KESVGNSTRIDYGTGHEAAFAAFLCCLCKIGVLRVDDQIAIVFKVFNRYLEVMRKLQKTY RMEPAGSQGVWGLDDFQFLPFIWGSSQLIDHPYLEPRHFVDEKAVNENHKDYMFLECILF ITEMKTGPFAEHSNQLWNISAVPSWSKVNQGLIRMYKAECLEKFPVIQHFKFGSLLPIHP VTS
Crystal Structure of the Pp2A Phosphatase Activator: Implications for its Pp2A-Specific Ppiase Activity. Leulliot, N., Vicentini, G., Jordens, J. et al. Mol Cell (2006) 23:413. DOI 10.1016/J.MOLCEL.2006.07.008 · PubMed
Other PDB entries of the same protein (UniProt Q15257 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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