9D7Q: Serine/threonine-protein kinase WNK3

Water and chloride as allosteric inhibitors in WNK kinase osmosensing. Determined by X-ray diffraction at 3.3 Å resolution. Released 11 Dec 2024.

Method: X-ray diffraction
Resolution: 3.3 Å
Organism: Homo sapiens
Chains: 2
Atoms: 4,372
Mol. weight: 64.13 kDa
Released: 11 Dec 2024

Explore 9D7Q in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

9D7Q contains 25 α-helices and 21 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.

Chain A: 13 helices, 11 β-strands

Element	Residues	Length	Sheet
β-strand	139-140	2	1
β-strand	146-155	10	1
β-strand	160-166	7	1
β-strand	171-177	7	1
α-helix	186-200	15
β-strand	203	1	2
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	297-300	4
α-helix	318-320	3
α-helix	327-343	17
α-helix	354-362	9
α-helix	365-367	3
α-helix	368-371	4
α-helix	376-386	11
α-helix	390-392	3
α-helix	396-400	5

Chain B: 12 helices, 10 β-strands

Element	Residues	Length	Sheet
β-strand	139-140	2	3
β-strand	146-154	9	3
β-strand	160-166	7	3
β-strand	171-177	7	3
α-helix	186-199	14
β-strand	206	1	4
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	297-300	4
α-helix	318-321	4
α-helix	328-343	16
α-helix	354-363	10
α-helix	368-371	4
α-helix	376-386	11
α-helix	394-395	2
α-helix	396-401	6

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Serine/threonine-protein kinase WNK3	A, B	protein	280	Homo sapiens	Q9BYP7 (AlphaFold model)

Sequence of entity 1 (A, B), FASTA

>9D7Q_1 Serine/threonine-protein kinase WNK3 (chains A, B)
EEEAEMKAVATSPSGRFLKFDIELGRGAFKTVYKGLDTETWVEVAWCELQDRKLTKAEQQ
RFKEEAEMLKGLQHPNIVRFYDSWESILKGKKCIVLVTELMTSGTLKTYLKRFKVMKPKV
LRSWCRQILKGLQFLHTRTPPIIHRDLKCNNIFITGPTGSVKIGDLGLATLMRTSFAKSV
IGTPAFMAPEMYEEHFDESVDVYAFGMCMLEMATSEYPYSECQNAAQIYRKVTSGIKPAS
FNKVTDPEVKEIIEGCIRQNKSERLSIRDLLNHAFFAEDT

Primary citation

Water and chloride as allosteric inhibitors in WNK kinase osmosensing. Teixeira, L.R., Akella, R., Humphreys, J.M. et al. Elife (2024) 12. DOI 10.7554/eLife.88224 · PubMed

Other PDB entries of the same protein (UniProt Q9BYP7 (AlphaFold model), which also has an AlphaFold model), best resolution first:

5O1V 1.72 Å, Crystal structure of WNK3 kinase domain in a monophosphorylated apo state (A-loop swapped)
5O2B 2.04 Å, Crystal structure of WNK3 kinase domain in a diphosphorylated state and in a complex…
5O21 2.06 Å, Crystal structure of WNK3 kinase domain in a monophosphorylated state with chloride…
5O23 2.25 Å, Crystal structure of WNK3 kinase domain in a monophosphorylated apo state
5O26 2.38 Å, Crystal structure of WNK3 kinase domain in a diphosphorylated state and in complex with…
5O2C 2.4 Å, Crystal structure of WNK3 kinase and CCT1 didomain in a unphosphorylated state
5NKP 2.8 Å, Crystal structure of the human KLHL3 Kelch domain in complex with a WNK3 peptide
8EDH 3.11 Å, Identification of a class of WNK isoform-specific inhibitors through high-throughput…

Browse structure collections

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