Crystal structure of CN:RII alpha. Determined by X-ray diffraction at 2.1 Å resolution. Released 17 Dec 2025.
Explore 9NXN in 3D Show helices and sheets RCSB PDB PDBe
9NXN contains 30 α-helices and 26 β-strands across 3 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 |
|---|---|---|---|
| α-helix | 22-25 | 4 | |
| β-strand | 29 | 1 | 1 |
| α-helix | 31-34 | 4 | |
| β-strand | 35 | 1 | 2 |
| β-strand | 41 | 1 | 2 |
| α-helix | 43-51 | 9 | |
| β-strand | 56 | 1 | 1 |
| α-helix | 58-73 | 16 | |
| β-strand | 78-81 | 4 | 3 |
| α-helix | 82 | 1 | |
| β-strand | 85-88 | 4 | 4 |
| α-helix | 95-105 | 11 | |
| β-strand | 113-115 | 3 | 4 |
| α-helix | 126-139 | 14 | |
| β-strand | 144-146 | 3 | 4 |
| α-helix | 154-159 | 6 | |
| α-helix | 162-169 | 8 | |
| α-helix | 172-183 | 12 | |
| β-strand | 188-191 | 4 | 3 |
| β-strand | 195-197 | 3 | 3 |
| β-strand | 203 | 1 | 5 |
| β-strand | 206 | 1 | 5 |
| α-helix | 210-213 | 4 | |
| α-helix | 220-222 | 3 | |
| α-helix | 226-232 | 7 | |
| β-strand | 234-235 | 2 | 6 |
| β-strand | 248-250 | 3 | 6 |
| β-strand | 258-260 | 3 | 6 |
| α-helix | 262-271 | 10 | |
| β-strand | 276-279 | 4 | 3 |
| β-strand | 288-290 | 3 | 3 |
| α-helix | 292 | 1 | |
| β-strand | 293 | 1 | 7 |
| α-helix | 294 | 1 | |
| β-strand | 300 | 1 | 7 |
| β-strand | 302-305 | 4 | 3 |
| α-helix | 311-313 | 3 | |
| β-strand | 319-325 | 7 | 4 |
| β-strand | 328-334 | 7 | 4 |
| α-helix | 344-346 | 3 | |
| α-helix | 349-369 | 21 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 6-9 | 4 | |
| α-helix | 16-29 | 14 | |
| β-strand | 36-37 | 2 | 8 |
| α-helix | 39-42 | 4 | |
| α-helix | 46-48 | 3 | |
| α-helix | 54-61 | 8 | |
| β-strand | 69-70 | 2 | 8 |
| α-helix | 71-79 | 9 | |
| α-helix | 87-98 | 12 | |
| β-strand | 105-106 | 2 | 9 |
| α-helix | 108-119 | 12 | |
| α-helix | 125-139 | 15 | |
| β-strand | 147-148 | 2 | 9 |
| α-helix | 149-156 | 8 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 86-88 | 3 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Serine/threonine-protein phosphatase 2B catalytic subunit alpha isoform | A | protein | 370 | Homo sapiens | Q08209 (AlphaFold model) |
| Calcineurin subunit B type 1 | B | protein | 170 | Homo sapiens | P63098 (AlphaFold model) |
| cAMP-dependent protein kinase type II-alpha regulatory subunit | C | protein | 64 | Homo sapiens | P13861 (AlphaFold model) |
>9NXN_1 Serine/threonine-protein phosphatase 2B catalytic subunit alpha isoform (chains A) MSEPKAIDPKLSTTDRVVKAVPFPPSHRLTAKEVFDNDGKPRVDILKAHLMKEGRLEESV ALRIITEGASILRQEKNLLDIDAPVTVCGDIHGQFFDLMKLFEVGGSPANTRYLFLGDYV DRGYFSIECVLYLWALKILYPKTLFLLRGNHECRHLTEYFTFKQECKIKYSERVYDACMD AFDCLPLAALMNQQFLCVHGGLSPEINTLDDIRKLDRFKEPPAYGPMCDILWSDPLEDFG NEKTQEHFTHNTVRGCSYFYSYPAVCEFLQHNNLLSILRAHEAQDAGYRMYRKSQTTGFP SLITIFSAPNYLDVYNNKAAVLKYENNVMNIRQFNCSPHPYWLPNFMDVFTWSLPFVGEK VTEMLVNVLN
>9NXN_2 Calcineurin subunit B type 1 (chains B) MGNEASYPLEMCSHFDADEIKRLGKRFKKLDLDNSGSLSVEEFMSLPELQQNPLVQRVID IFDTDGNGEVDFKEFIEGVSQFSVKGDKEQKLRFAFRIYDMDKDGYISNGELFQVLKMMV GNNLKDTQLQQIVDKTIINADKDGDGRISFEEFCAVVGGLDIHKKMVVDV
>9NXN_3 cAMP-dependent protein kinase type II-alpha regulatory subunit (chains C) GHMWRAPASVLPAATPRQSLGHPPPEPGPDRVADAKGDSESEEDEDLEVPVPSRFNRRVS VCAE
| ID | Name | Formula | Copies |
|---|---|---|---|
| CA | Calcium ion | Ca | 4 |
The clinical missense variant E282K in PPP3CA/calcineurin shifts substrate dephosphorylation by altering active site recruitment. Shirakawa, K.T., Parikh, T., Machado, L.E.S.F. et al. Nat Commun (2026) 17. DOI 10.1038/s41467-026-69535-5 · PubMed
Other PDB entries of the same protein (UniProt Q08209 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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