Crystal structure of WNK3 kinase domain in a diphosphorylated state and in complex with AMP-PNP/Mg2+. Determined by X-ray diffraction at 2.38 Å resolution. Released 28 Jun 2017.
Explore 5O26 in 3D Show helices and sheets RCSB PDB PDBe
5O26 contains 31 α-helices and 28 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 | 139-140 | 2 | 1 |
| β-strand | 146-155 | 10 | 1 |
| β-strand | 159-166 | 8 | 1 |
| β-strand | 171-179 | 9 | 1 |
| α-helix | 185-198 | 14 | |
| β-strand | 206 | 1 | 2 |
| β-strand | 209-215 | 7 | 1 |
| β-strand | 222-228 | 7 | 1 |
| β-strand | 234 | 1 | 2 |
| α-helix | 235-242 | 8 | |
| α-helix | 245-246 | 2 | |
| α-helix | 247-265 | 19 | |
| β-strand | 271-272 | 2 | 3 |
| α-helix | 278-280 | 3 | |
| β-strand | 281-284 | 4 | 2 |
| β-strand | 289-292 | 4 | 2 |
| α-helix | 295-297 | 3 | |
| β-strand | 299-300 | 2 | 3 |
| β-strand | 306 | 1 | 4 |
| α-helix | 313-315 | 3 | |
| α-helix | 318-320 | 3 | |
| β-strand | 325 | 1 | 4 |
| α-helix | 328-343 | 16 | |
| α-helix | 354-362 | 9 | |
| α-helix | 365-367 | 3 | |
| α-helix | 368-372 | 5 | |
| α-helix | 376-385 | 10 | |
| α-helix | 390-392 | 3 | |
| α-helix | 394-395 | 2 | |
| α-helix | 396-400 | 5 | |
| α-helix | 404-406 | 3 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 137-140 | 4 | 5 |
| β-strand | 146-155 | 10 | 5 |
| β-strand | 159-166 | 8 | 5 |
| β-strand | 171-178 | 8 | 5 |
| α-helix | 188-199 | 12 | |
| β-strand | 206 | 1 | 6 |
| β-strand | 209-214 | 6 | 5 |
| β-strand | 223-228 | 6 | 5 |
| β-strand | 234 | 1 | 6 |
| α-helix | 235-242 | 8 | |
| α-helix | 247-265 | 19 | |
| β-strand | 271-272 | 2 | 7 |
| α-helix | 278-280 | 3 | |
| β-strand | 281-283 | 3 | 6 |
| β-strand | 290-292 | 3 | 6 |
| α-helix | 295-297 | 3 | |
| β-strand | 299-300 | 2 | 7 |
| β-strand | 306 | 1 | 8 |
| α-helix | 313-315 | 3 | |
| α-helix | 318-320 | 3 | |
| β-strand | 325 | 1 | 8 |
| α-helix | 328-343 | 16 | |
| α-helix | 354-362 | 9 | |
| α-helix | 368-372 | 5 | |
| α-helix | 376-385 | 10 | |
| α-helix | 394-395 | 2 | |
| α-helix | 396-400 | 5 | |
| α-helix | 403-406 | 4 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Serine/threonine-protein kinase WNK3 | A, B | protein | 284 | Homo sapiens | Q9BYP7 (AlphaFold model) |
>5O26_1 Serine/threonine-protein kinase WNK3 (chains A, B) SMAEMKAVATSPSGRFLKFDIELGRGAFKTVYKGLDTETWVEVAWCELQDRKLTKAEQQR FKEEAEMLKGLQHPNIVRFYDSWESILKGKKCIVLVTELMTSGTLKTYLKRFKVMKPKVL RSWCRQILKGLQFLHTRTPPIIHRDLKCDNIFITGPTGSVKIGDLGLATLMRTSFAKSVI GTPEFMAPEMYEEHYDESVDVYAFGMCMLEMATSEYPYSECQNAAQIYRKVTSGIKPASF NKVTDPEVKEIIEGCIRQNKSERLSIRDLLNHAFFAEDTGLRVE
| ID | Name | Formula | Copies |
|---|---|---|---|
| MG | Magnesium ion | Mg | 4 |
| ANP | Phosphoaminophosphonic acid-adenylate ester | C10 H17 N6 O12 P3 | 2 |
Water and common crystallization additives (EDO) are not listed.
Crystal structure of WNK3 kinase domain in a diphosphorylated state and in complex with AMP-PNP/Mg2+. Pinkas, D.M., Daubner, G.M., Bufton, J.C. et al. To be published.
Other PDB entries of the same protein (UniProt Q9BYP7 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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