4CH9: Human KLHL3 Kelch domain

Crystal structure of the human KLHL3 Kelch domain in complex with a WNK4 peptide. Determined by X-ray diffraction at 1.84 Å resolution. Released 8 Jan 2014.

Method: X-ray diffraction
Resolution: 1.84 Å
Organism: HOMO SAPIENS
Chains: 4
Atoms: 5,096
Mol. weight: 66.16 kDa
Released: 8 Jan 2014

Explore 4CH9 in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

4CH9 contains 14 α-helices and 84 β-strands across 4 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: 6 helices, 40 β-strands

Element	Residues	Length	Sheet
β-strand	301-306	6	1
β-strand	309	1	2
β-strand	313	1	2
β-strand	317-321	5	1
β-strand	326-330	5	1
α-helix	332-333	2
β-strand	338	1	3
β-strand	341-345	5	3
β-strand	348-355	8	3
β-strand	360-368	9	3
β-strand	373-376	4	3
α-helix	378-380	3
β-strand	385	1	4
β-strand	388-392	5	5
β-strand	395-399	5	5
β-strand	402	1	4
β-strand	407	1	4
β-strand	411-415	5	5
β-strand	420-424	5	5
α-helix	425-427	3
β-strand	432	1	6
β-strand	435-439	5	7
β-strand	442-446	5	7
β-strand	449-450	2	6
β-strand	455-456	2	6
β-strand	460-464	5	7
β-strand	469-472	4	7
α-helix	474-476	3
β-strand	481	1	8
β-strand	484-488	5	9
β-strand	491-495	5	9
β-strand	498-499	2	8
β-strand	502-503	2	8
β-strand	507-511	5	9
β-strand	516-520	5	9
α-helix	521-523	3
β-strand	528	1	10
β-strand	531-535	5	11
β-strand	538-542	5	11
β-strand	545	1	10
β-strand	550	1	10
α-helix	551	1
β-strand	554-558	5	11
β-strand	563-566	4	11
β-strand	576	1	2
β-strand	579-584	6	1

Chain B: 6 helices, 44 β-strands

Element	Residues	Length	Sheet
β-strand	301-306	6	12
β-strand	309	1	13
β-strand	313	1	13
β-strand	314	1	14
β-strand	317-321	5	12
β-strand	326-330	5	12
α-helix	331-333	3
β-strand	337	1	14
β-strand	338	1	15
β-strand	341-345	5	16
β-strand	348-352	5	16
β-strand	355	1	15
β-strand	360	1	15
β-strand	364-368	5	16
β-strand	373-377	5	16
α-helix	378-380	3
β-strand	385	1	17
β-strand	388-392	5	18
β-strand	395-399	5	18
β-strand	402	1	17
β-strand	407	1	17
β-strand	411-415	5	18
β-strand	420-424	5	18
α-helix	425-427	3
β-strand	432	1	19
β-strand	435-439	5	20
β-strand	442-446	5	20
β-strand	449-450	2	19
β-strand	455-456	2	19
β-strand	460-464	5	20
β-strand	469-472	4	20
α-helix	474-476	3
β-strand	481	1	21
β-strand	484-488	5	22
β-strand	491-495	5	22
β-strand	498-499	2	21
β-strand	502-503	2	21
β-strand	507-511	5	22
β-strand	516-520	5	22
α-helix	521-523	3
β-strand	528	1	23
β-strand	531-535	5	24
β-strand	538-542	5	24
β-strand	545	1	23
β-strand	550	1	23
α-helix	551	1
β-strand	554-558	5	24
β-strand	563-566	4	24
β-strand	576	1	13
β-strand	579-584	6	12

Chains C and D: 1 helix, 0 β-strands

Element	Residues	Length	Sheet
α-helix	562-564	3

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Kelch-like protein 3	A, B	protein	292	HOMO SAPIENS	Q9UH77 (AlphaFold model)
Serine/threonine-protein kinase WNK4	C, D	protein	11	HOMO SAPIENS	Q96J92 (AlphaFold model)

Sequence of entity 1 (A, B), FASTA

>4CH9_1 KELCH-LIKE PROTEIN 3 (chains A, B)
SMSLPKVMIVVGGQAPKAIRSVECYDFEEDRWDQIAELPSRRCRAGVVFMAGHVYAVGGF
NGSLRVRTVDVYDGVKDQWTSIASMQERRSTLGAAVLNDLLYAVGGFDGSTGLASVEAYS
YKTNEWFFVAPMNTRRSSVGVGVVEGKLYAVGGYDGASRQCLSTVEQYNPATNEWIYVAD
MSTRRSGAGVGVLSGQLYATGGHDGPLVRKSVEVYDPGTNTWKQVADMNMCRRNAGVCAV
NGLLYVVGGDDGSCNLASVEYYNPVTDKWTLLPTNMSTGRSYAGVAVIHKSL

Sequence of entity 2 (C, D), FASTA

>4CH9_2 SERINE/THREONINE-PROTEIN KINASE WNK4 (chains C, D)
EPEEPEADQHQ

Primary citation

Structural and Biochemical Characterisation of the Klhl3-Wnk Kinase Interaction Important in Blood Pressure Regulation. Schumacher, F., Sorrell, F.J., Alessi, D.R. et al. Biochem J (2014) 460:237. DOI 10.1042/BJ20140153 · PubMed

Other PDB entries of the same protein (UniProt Q9UH77 (AlphaFold model), which also has an AlphaFold model), best resolution first:

5NKP 2.8 Å, Crystal structure of the human KLHL3 Kelch domain in complex with a WNK3 peptide
4HXI 3.51 Å, Crystal structure of KLHL3/Cul3 complex

Browse structure collections

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