8KHP: CULLIN3-KLHL22-RBX1 E3 ligase

CULLIN3-KLHL22-RBX1 E3 ligase. Determined by electron microscopy at 3.67 Å resolution. Released 13 Dec 2023.

Method: Electron microscopy
Resolution: 3.67 Å
Organism: Homo sapiens
Chains: 6
Atoms: 16,023
Mol. weight: 346.2 kDa
Released: 13 Dec 2023

Explore 8KHP in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

8KHP contains 137 α-helices and 90 β-strands across 6 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: 26 helices, 36 β-strands

Element	Residues	Length	Sheet
β-strand	26-28	3	1
α-helix	33-46	14
β-strand	52-56	5	2
β-strand	59-63	5	2
α-helix	65-71	7
α-helix	74-80	7
α-helix	84-87	4
β-strand	90-92	3	2
α-helix	98-110	13
β-strand	112-114	3	3
α-helix	120-129	10
α-helix	133-144	12
α-helix	152-161	10
α-helix	171-177	7
α-helix	179-183	5
α-helix	186-190	5
α-helix	193-201	9
α-helix	212-221	10
α-helix	224-227	4
α-helix	239-243	5
α-helix	246-248	3
α-helix	251-253	3
α-helix	254-260	7
α-helix	266-277	12
α-helix	289-291	3
β-strand	298-301	4	4
β-strand	322	1	5
β-strand	327	1	5
β-strand	345-346	2	6
β-strand	351-353	3	6
β-strand	369-373	5	6
β-strand	378-382	5	6
α-helix	383-385	3
β-strand	390	1	7
β-strand	393-395	3	8
β-strand	401-404	4	8
β-strand	407	1	7
β-strand	412	1	7
β-strand	417-420	4	8
β-strand	425-428	4	8
α-helix	430-432	3
β-strand	440-444	5	9
β-strand	447-451	5	9
β-strand	453-455	3	10
β-strand	458-460	3	10
β-strand	464-467	4	9
β-strand	472-475	4	9
α-helix	477-479	3
β-strand	487-491	5	11
β-strand	494-498	5	11
α-helix	503-505	3
β-strand	517-518	2	12
β-strand	523-524	2	12
α-helix	528-530	3
β-strand	538-542	5	13
β-strand	545-549	5	13
β-strand	552-553	2	14
β-strand	558-559	2	14
β-strand	564-567	4	13
β-strand	572-575	4	13
β-strand	589-592	4	4
α-helix	595-599	5

Chain B: 28 helices, 45 β-strands

Element	Residues	Length	Sheet
β-strand	26-28	3	3
α-helix	32-46	15
β-strand	52-56	5	15
β-strand	59-63	5	15
α-helix	65-69	5
α-helix	74-80	7
α-helix	84-87	4
β-strand	90-93	4	15
α-helix	98-110	13
β-strand	112-114	3	1
α-helix	120-130	11
α-helix	133-145	13
α-helix	149-151	3
α-helix	152-161	10
α-helix	165-177	13
α-helix	179-184	6
α-helix	187-190	4
α-helix	193-201	9
α-helix	210-221	12
α-helix	224-227	4
α-helix	240-243	4
α-helix	246-248	3
α-helix	251-260	10
α-helix	265-277	13
α-helix	280-282	3
α-helix	289-291	3
β-strand	297-303	7	16
β-strand	306-307	2	17
β-strand	314	1	17
β-strand	317-322	6	16
β-strand	327-332	6	16
α-helix	342	1
β-strand	343-347	5	18
β-strand	350-354	5	18
β-strand	371-372	2	18
β-strand	373	1	19
β-strand	378	1	19
β-strand	390	1	20
β-strand	394-397	4	21
β-strand	400-403	4	21
β-strand	407	1	20
β-strand	412	1	20
β-strand	413	1	22
β-strand	417-420	4	21
β-strand	425-428	4	21
α-helix	430-432	3
β-strand	436	1	22
β-strand	440-443	4	23
β-strand	448-451	4	23
β-strand	454-455	2	24
β-strand	458-459	2	24
β-strand	464-466	3	23
β-strand	467	1	25
β-strand	472	1	25
α-helix	477-479	3
β-strand	488-491	4	26
β-strand	494-497	4	26
α-helix	503-505	3
β-strand	515-518	4	26
β-strand	523-526	4	26
α-helix	528-530	3
β-strand	535	1	27
α-helix	537	1
β-strand	538-541	4	17
β-strand	545	1	28
β-strand	546-549	4	17
β-strand	552-553	2	27
β-strand	558-559	2	27
β-strand	560-566	7	17
β-strand	567	1	28
β-strand	573-584	12	17
β-strand	587-593	7	16
α-helix	595-598	4

Chain C: 41 helices, 5 β-strands

Element	Residues	Length	Sheet
α-helix	20-22	3
α-helix	29-45	17
α-helix	54-66	13
α-helix	70-84	15
α-helix	85-89	5
α-helix	90-93	4
α-helix	94-96	3
α-helix	101-122	22
α-helix	124-126	3
α-helix	127-131	5
α-helix	132-134	3
α-helix	139-147	9
α-helix	148-152	5
α-helix	155-173	19
α-helix	181-193	13
α-helix	199-201	3
α-helix	202-206	5
α-helix	207-227	21
α-helix	230-250	21
α-helix	254-256	3
α-helix	257-269	13
α-helix	270-272	3
α-helix	273-278	6
α-helix	284-290	7
α-helix	293-302	10
α-helix	309-328	20
α-helix	338-359	22
α-helix	364-378	15
α-helix	384-396	13
α-helix	405-421	17
α-helix	425-442	18
α-helix	448-462	15
α-helix	464-493	30
β-strand	508	1	29
α-helix	526-542	17
β-strand	549	1	29
β-strand	557-559	3	30
β-strand	592-594	3	30
α-helix	596-607	12
α-helix	613-620	8
α-helix	624-634	11
β-strand	672-673	2	30
α-helix	674-676	3
α-helix	685-714	30
α-helix	719-729	11
α-helix	738-750	13

Chain D: 39 helices, 2 β-strands

Element	Residues	Length	Sheet
α-helix	18-20	3
α-helix	27-45	19
α-helix	55-66	12
α-helix	70-85	16
α-helix	86-90	5
α-helix	91-95	5
α-helix	101-122	22
α-helix	124-134	11
α-helix	139-147	9
α-helix	148-152	5
α-helix	157-174	18
α-helix	180-192	13
α-helix	199-200	2
α-helix	201-206	6
α-helix	207-227	21
α-helix	230-250	21
α-helix	258-264	7
α-helix	265-270	6
α-helix	273-277	5
α-helix	284-290	7
α-helix	294-305	12
α-helix	309-328	20
α-helix	338-360	23
α-helix	364-379	16
α-helix	384-395	12
α-helix	406-420	15
α-helix	425-441	17
α-helix	449-462	14
α-helix	464-493	30
α-helix	510-512	3
α-helix	530-542	13
β-strand	557-559	3	31
β-strand	592-594	3	31
α-helix	599-607	9
α-helix	613-620	8
α-helix	624-635	12
α-helix	659-661	3
α-helix	685-714	30
α-helix	719-731	13
α-helix	738-746	9
α-helix	749-751	3

Chain E: 1 helix, 2 β-strands

Element	Residues	Length	Sheet
α-helix	81-88	8
β-strand	93	1	32
β-strand	100	1	32

Chain F: 2 helices, 0 β-strands

Element	Residues	Length	Sheet
α-helix	81-85	5
α-helix	86-90	5

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Kelch-like protein 22	A, B	protein	634	Homo sapiens	Q53GT1 (AlphaFold model)
Cullin-3	C, D	protein	768	Homo sapiens	Q13618 (AlphaFold model)
E3 ubiquitin-protein ligase RBX1	E, F	protein	108	Homo sapiens	P62877 (AlphaFold model)

Sequence of entity 1 (A, B), FASTA

>8KHP_1 Kelch-like protein 22 (chains A, B)
MAEEQEFTQLCKLPAQPSHPHCVNNTYRSAQHSQALLRGLLALRDSGILFDVVLVVEGRH
IEAHRILLAASCDYFRGMFAGGLKEMEQEEVLIHGVSYNAMCQILHFIYTSELELSLSNV
QETLVAACQLQIPEIIHFCCDFLMSWVDEENILDVYRLAELFDLSRLTEQLDTYILKNFV
AFSRTDKYRQLPLEKVYSLLSSNRLEVSCETEVYEGALLYHYSLEQVQADQISLHEPPKL
LETVRFPLMEAEVLQRLHDKLDPSPLRDTVASALMYHRNESLQPSLQSPQTELRSDFQCV
VGFGGIHSTPSTVLSDQAKYLNPLLGEWKHFTASLAPRMSNQGIAVLNNFVYLIGGDNNV
QGFRAESRCWRYDPRHNRWFQIQSLQQEHADLSVCVVGRYIYAVAGRDYHNDLNAVERYD
PATNSWAYVAPLKREVYAHAGATLEGKMYITCGRRGEDYLKETHCYDPGSNTWHTLADGP
VRRAWHGMATLLNKLYVIGGSNNDAGYRRDVHQVACYSCTSGQWSSVCPLPAGHGEPGIA
VLDNRIYVLGGRSHNRGSRTGYVHIYDVEKDCWEEGPQLDNSISGLAACVLTLPRSLLLE
PPRGTPDRSQADPDFASEVMSVSDWEEFDNSSED

Sequence of entity 2 (C, D), FASTA

>8KHP_2 Cullin-3 (chains C, D)
MSNLSKGTGSRKDTKMRIRAFPMTMDEKYVNSIWDLLKNAIQEIQRKNNSGLSFEELYRN
AYTMVLHKHGEKLYTGLREVVTEHLINKVREDVLNSLNNNFLQTLNQAWNDHQTAMVMIR
DILMYMDRVYVQQNNVENVYNLGLIIFRDQVVRYGCIRDHLRQTLLDMIARERKGEVVDR
GAIRNACQMLMILGLEGRSVYEEDFEAPFLEMSAEFFQMESQKFLAENSASVYIKKVEAR
INEEIERVMHCLDKSTEEPIVKVVERELISKHMKTIVEMENSGLVHMLKNGKTEDLGCMY
KLFSRVPNGLKTMCECMSSYLREQGKALVSEEGEGKNPVDYIQGLLDLKSRFDRFLLESF
NNDRLFKQTIAGDFEYFLNLNSRSPEYLSLFIDDKLKKGVKGLTEQEVETILDKAMVLFR
FMQEKDVFERYYKQHLARRLLTNKSVSDDSEKNMISKLKTECGCQFTSKLEGMFRDMSIS
NTTMDEFRQHLQATGVSLGGVDLTVRVLTTGYWPTQSATPKCNIPPAPRHAFEIFRRFYL
AKHSGRQLTLQHHMGSADLNATFYGPVKKEDGSEVGVGGAQVTGSNTRKHILQVSTFQMT
ILMLFNNREKYTFEEIQQETDIPERELVRALQSLACGKPTQRVLTKEPKSKEIENGHIFT
VNDQFTSKLHRVKIQTVAAKQGESDPERKETRQKVDDDRKHEIEAAIVRIMKSRKKMQHN
VLVAEVTQQLKARFLPSPVVIKKRIEGLIEREYLARTPEDRKVYTYVA

Sequence of entity 3 (E, F), FASTA

>8KHP_3 E3 ubiquitin-protein ligase RBX1 (chains E, F)
MAAAMDVDTPSGTNSGAGKKRFEVKKWNAVALWAWDIVVDNCAICRNHIMDLCIECQANQ
ASATSEECTVAWGVCNHAFHFHCISRWLKTRQVCPLDNREWEFQKYGH

Primary citation

Cryo-EM structure of the KLHL22 E3 ligase bound to an oligomeric metabolic enzyme. Teng, F., Wang, Y., Liu, M. et al. Structure (2023) 31:1431-1440.e5. DOI 10.1016/j.str.2023.09.002 · PubMed

Other PDB entries of the same protein (UniProt Q53GT1 (AlphaFold model), which also has an AlphaFold model), best resolution first:

8W4J 3.06 Å, Cryo-EM structure of the KLHL22 E3 ligase bound to human glutamate dehydrogenase I
8K8T 3.8 Å, Structure of CUL3-RBX1-KLHL22 complex
8K9I 4.2 Å, Structure of CUL3-RBX1-KLHL22 complex without CUL3 NA motif

Browse structure collections

About this viewer

MolViewer shows 8KHP directly in your browser with nothing to install. Switch between cartoon, ball-and-stick, spacefill and surface views, color by chain, secondary structure or B-factor, measure distances, angles and dihedrals, and share or embed the view.