Crystal structure of the phosphotyrosyl phosphatase activator. Determined by X-ray diffraction at 1.9 Å resolution. Released 22 Aug 2006.
Explore 2HV6 in 3D Show helices and sheets RCSB PDB PDBe
2HV6 contains 47 α-helices and 14 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 | 27-28 | 2 | 1 |
| α-helix | 35-41 | 7 | |
| β-strand | 42 | 1 | 2 |
| α-helix | 43-59 | 17 | |
| α-helix | 72-90 | 19 | |
| α-helix | 92-95 | 4 | |
| α-helix | 104-120 | 17 | |
| 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 | 207-210 | 4 | |
| α-helix | 218-227 | 10 | |
| α-helix | 235-239 | 5 | |
| α-helix | 241-247 | 7 | |
| 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 | 1 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 27-28 | 2 | 4 |
| α-helix | 34-38 | 5 | |
| β-strand | 42 | 1 | 5 |
| α-helix | 43-59 | 17 | |
| α-helix | 69-71 | 3 | |
| α-helix | 74-90 | 17 | |
| α-helix | 92-94 | 3 | |
| α-helix | 104-120 | 17 | |
| α-helix | 126-131 | 6 | |
| α-helix | 132-140 | 9 | |
| β-strand | 145 | 1 | 6 |
| β-strand | 150-151 | 2 | 6 |
| α-helix | 153-168 | 16 | |
| α-helix | 177-179 | 3 | |
| α-helix | 180-185 | 6 | |
| α-helix | 186-199 | 14 | |
| α-helix | 201 | 1 | |
| β-strand | 202-203 | 2 | 6 |
| α-helix | 212-215 | 4 | |
| α-helix | 218-227 | 10 | |
| α-helix | 235-239 | 5 | |
| α-helix | 241-247 | 7 | |
| α-helix | 252-262 | 11 | |
| α-helix | 274-279 | 6 | |
| α-helix | 284-296 | 13 | |
| α-helix | 299-301 | 3 | |
| α-helix | 303-306 | 4 | |
| β-strand | 310-311 | 2 | 4 |
| β-strand | 319 | 1 | 5 |
| α-helix | 320 | 1 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Protein phosphatase 2A, regulatory subunit B | A, B | protein | 323 | Homo sapiens | Q15257 (AlphaFold model) |
>2HV6_1 Protein phosphatase 2A, regulatory subunit B (chains A, B) MAEGERQPPPDSSEEAPPATQNFIIPKKEIHTVPDMGKWKRSQAYADYIGFILTLNEGVK GKKLTFEYRVSEAIEKLVALLNTLDRWIDETPPVDQPSRFGNKAYRTWYAKLDEEAENLV ATVVPTHLAAAVPEVAVYLKESVGNSTRIDYGTGHEAAFAAFLCCLCKIGVLRVDDQIAI VFKVFNRYLEVMRKLQKTYRMEPAGSQGVWGLDDFQFLPFIWGSSQLIDHPYLEPRHFVD EKAVNENHKDYMFLECILFITEMKTGPFAEHSNQLWNISAVPSWSKVNQGLIRMYKAECL EKFPVIQHFKFGSLLPIHPVTSG
| ID | Name | Formula | Copies |
|---|---|---|---|
| MG | Magnesium ion | Mg | 1 |
Structure and mechanism of the phosphotyrosyl phosphatase activator. Chao, Y., Xing, Y., Chen, Y. et al. Mol Cell (2006) 23:535-546. DOI 10.1016/j.molcel.2006.07.027 · 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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