Crystal structure of WNK3 kinase domain in a monophosphorylated state with chloride bound in the active site. Determined by X-ray diffraction at 2.06 Å resolution. Released 28 Jun 2017.
Explore 5O21 in 3D Show helices and sheets RCSB PDB PDBe
5O21 contains 34 α-helices and 20 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 | 140 | 1 | 1 |
| β-strand | 146-156 | 11 | 1 |
| β-strand | 159-166 | 8 | 1 |
| β-strand | 171-178 | 8 | 1 |
| α-helix | 185-197 | 13 | |
| α-helix | 198-200 | 3 | |
| β-strand | 206 | 1 | 2 |
| β-strand | 209-217 | 9 | 1 |
| β-strand | 220-228 | 9 | 1 |
| β-strand | 234 | 1 | 2 |
| α-helix | 235-242 | 8 | |
| α-helix | 247-265 | 19 | |
| α-helix | 278-280 | 3 | |
| β-strand | 281-283 | 3 | 2 |
| β-strand | 290-292 | 3 | 2 |
| α-helix | 295-298 | 4 | |
| α-helix | 299-302 | 4 | |
| α-helix | 304-310 | 7 | |
| α-helix | 318-321 | 4 | |
| α-helix | 328-343 | 16 | |
| α-helix | 354-362 | 9 | |
| 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 | 403-405 | 3 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 137-140 | 4 | 3 |
| β-strand | 146-156 | 11 | 3 |
| β-strand | 159-166 | 8 | 3 |
| β-strand | 172-178 | 7 | 3 |
| α-helix | 185-199 | 15 | |
| β-strand | 206 | 1 | 4 |
| α-helix | 207-208 | 2 | |
| β-strand | 209-217 | 9 | 3 |
| β-strand | 220-228 | 9 | 3 |
| β-strand | 234 | 1 | 4 |
| α-helix | 235-242 | 8 | |
| α-helix | 247-265 | 19 | |
| α-helix | 278-280 | 3 | |
| β-strand | 281-283 | 3 | 4 |
| β-strand | 290-292 | 3 | 4 |
| α-helix | 295-298 | 4 | |
| α-helix | 299-302 | 4 | |
| α-helix | 304-310 | 7 | |
| α-helix | 313-315 | 3 | |
| α-helix | 318-321 | 4 | |
| 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 | 403-405 | 3 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Serine/threonine-protein kinase WNK3 | A, B | protein | 285 | Homo sapiens | Q9BYP7 (AlphaFold model) |
>5O21_1 Serine/threonine-protein kinase WNK3 (chains A, B) SMEAEMKAVATSPSGRFLKFDIELGRGAFKTVYKGLDTETWVEVAWCELQDRKLTKAEQQ RFKEEAEMLKGLQHPNIVRFYDSWESILKGKKCIVLVTELMTSGTLKTYLKRFKVMKPKV LRSWCRQILKGLQFLHTRTPPIIHRDLKCDNIFITGPTGSVKIGDLGLATLMRTSFAKSV IGTPEFMAPEMYEEHYDESVDVYAFGMCMLEMATSEYPYSECQNAAQIYRKVTSGIKPAS FNKVTDPEVKEIIEGCIRQNKSERLSIRDLLNHAFFAEDTGLRVE
Crystal structure of WNK3 kinase domain in a monophosphorylated state with chloride bound in the active site. 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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