Crystal Structure of Calcineurin Clinical Variant E282K. Determined by X-ray diffraction at 2.09 Å resolution. Released 17 Dec 2025.
Explore 9NXE in 3D Show helices and sheets RCSB PDB PDBe
9NXE contains 29 α-helices and 29 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 | 28-29 | 2 | 1 |
| α-helix | 31-34 | 4 | |
| β-strand | 35 | 1 | 2 |
| β-strand | 41 | 1 | 2 |
| α-helix | 43-51 | 9 | |
| β-strand | 55-56 | 2 | 1 |
| α-helix | 58-73 | 16 | |
| β-strand | 78-81 | 4 | 3 |
| α-helix | 82 | 1 | |
| β-strand | 85-88 | 4 | 4 |
| β-strand | 90 | 1 | 5 |
| 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 | 6 |
| β-strand | 206 | 1 | 6 |
| α-helix | 209-213 | 5 | |
| α-helix | 220-222 | 3 | |
| α-helix | 226-232 | 7 | |
| β-strand | 234-235 | 2 | 7 |
| β-strand | 248-250 | 3 | 7 |
| β-strand | 258-260 | 3 | 7 |
| α-helix | 262-271 | 10 | |
| β-strand | 276-279 | 4 | 3 |
| β-strand | 288-290 | 3 | 3 |
| α-helix | 291-292 | 2 | |
| β-strand | 293 | 1 | 8 |
| α-helix | 294 | 1 | |
| β-strand | 300 | 1 | 8 |
| β-strand | 302-305 | 4 | 3 |
| β-strand | 306 | 1 | 5 |
| 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 | 17-30 | 14 | |
| β-strand | 37-38 | 2 | 9 |
| α-helix | 40-44 | 5 | |
| α-helix | 47-49 | 3 | |
| α-helix | 55-62 | 8 | |
| β-strand | 70-71 | 2 | 9 |
| α-helix | 72-80 | 9 | |
| α-helix | 88-99 | 12 | |
| β-strand | 106-107 | 2 | 10 |
| α-helix | 109-120 | 12 | |
| α-helix | 126-140 | 15 | |
| β-strand | 148-149 | 2 | 10 |
| α-helix | 150-156 | 7 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 713-715 | 3 | |
| β-strand | 716-720 | 5 | 4 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Protein phosphatase 3 catalytic subunit alpha | A | protein | 370 | Homo sapiens | Q08209 (AlphaFold model) |
| Calcineurin subunit B type 1 | B | protein | 156 | Homo sapiens | P63098 (AlphaFold model) |
| Sodium/hydrogen exchanger 1 | C | protein | 48 | Homo sapiens | P19634 (AlphaFold model) |
>9NXE_1 Protein phosphatase 3 catalytic subunit alpha (chains A) MSEPKAIDPKLSTTDRVVKAVPFPPSHRLTAKEVFDNDGKPRVDILKAHLMKEGRLEESV ALRIITEGASILRQEKNLLDIDAPVTVCGDIHGQFFDLMKLFEVGGSPANTRYLFLGDYV DRGYFSIECVLYLWALKILYPKTLFLLRGNHECRHLTEYFTFKQECKIKYSERVYDACMD AFDCLPLAALMNQQFLCVHGGLSPEINTLDDIRKLDRFKEPPAYGPMCDILWSDPLEDFG NEKTQEHFTHNTVRGCSYFYSYPAVCEFLQHNNLLSILRAHKAQDAGYRMYRKSQTTGFP SLITIFSAPNYLDVYNNKAAVLKYENNVMNIRQFNCSPHPYWLPNFMDVFTWSLPFVGEK VTEMLVNVLN
>9NXE_2 Calcineurin subunit B type 1 (chains B) MDADEIKRLGKRFKKLDLDNSGSLSVEEFMSLPELQQNPLVQRVIDIFDTDGNGEVDFKE FIEGVSQFSVKGDKEQKLRFAFRIYDMDKDGYISNGELFQVLKMMVGNNLKDTQLQQIVD KTIINADKDGDGRISFEEFCAVVGGLDIHKKMVVDV
>9NXE_3 Sodium/hydrogen exchanger 1 (chains C) GHMKINNYLTVPAHKLDSPTMSRARIGSDPLAYEPKEDLPVITIDPAS
Water and common crystallization additives (PEG) are not listed.
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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