8K8T: CUL3-RBX1-KLHL22 complex

Name: PDB 8K8T: Structure of CUL3-RBX1-KLHL22 complex
Published: 2024-05-22
License: https://creativecommons.org/publicdomain/zero/1.0/
Keywords: ligase

Structure of CUL3-RBX1-KLHL22 complex. Determined by electron microscopy at 3.8 Å resolution. Released 22 May 2024.

Method: Electron microscopy
Resolution: 3.8 Å
Organism: Homo sapiens
Chains: 4
Atoms: 9,926
Mol. weight: 330.23 kDa
Released: 22 May 2024

Explore 8K8T in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

8K8T contains 72 α-helices and 10 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 C: 28 helices, 0 β-strands

Element	Residues	Length
α-helix	30-45	16
α-helix	49-51	3
α-helix	54-66	13
α-helix	70-85	16
α-helix	86-90	5
α-helix	91-94	4
α-helix	104-122	19
α-helix	126-130	5
α-helix	139-150	12
α-helix	157-173	17
α-helix	180-192	13
α-helix	199-201	3
α-helix	202-206	5
α-helix	207-224	18
α-helix	231-251	21
α-helix	257-264	8
α-helix	265-269	5
α-helix	273-276	4
α-helix	293-303	11
α-helix	309-329	21
α-helix	338-354	17
α-helix	355-359	5
α-helix	364-377	14
α-helix	384-396	13
α-helix	405-421	17
α-helix	431-438	8
α-helix	448-458	11
α-helix	465-479	15

Chain D: 28 helices, 0 β-strands

Element	Residues	Length
α-helix	30-45	16
α-helix	49-51	3
α-helix	54-67	14
α-helix	70-85	16
α-helix	86-90	5
α-helix	91-94	4
α-helix	103-122	20
α-helix	126-130	5
α-helix	139-150	12
α-helix	157-173	17
α-helix	181-192	12
α-helix	199-201	3
α-helix	202-206	5
α-helix	207-224	18
α-helix	231-250	20
α-helix	254-256	3
α-helix	257-264	8
α-helix	265-269	5
α-helix	273-277	5
α-helix	293-303	11
α-helix	309-329	21
α-helix	338-358	21
α-helix	364-380	17
α-helix	384-396	13
α-helix	405-421	17
α-helix	425-441	17
α-helix	448-458	11
α-helix	465-479	15

Chain K: 8 helices, 5 β-strands

Element	Residues	Length	Sheet
β-strand	25-28	4	1
α-helix	31-46	16
β-strand	52-55	4	2
β-strand	60-63	4	2
α-helix	67-69	3
α-helix	73-79	7
β-strand	90-92	3	2
α-helix	98-110	13
β-strand	112-113	2	3
α-helix	123-130	8
α-helix	133-145	13
α-helix	152-162	11
α-helix	165-177	13

Chain L: 8 helices, 5 β-strands

Element	Residues	Length	Sheet
β-strand	27-28	2	3
α-helix	31-46	16
β-strand	52-55	4	4
β-strand	60-63	4	4
α-helix	67-70	4
α-helix	73-79	7
β-strand	90-92	3	4
α-helix	98-110	13
β-strand	112-115	4	1
α-helix	123-130	8
α-helix	133-145	13
α-helix	152-162	11
α-helix	165-177	13

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Cullin-3	C, D	protein	776	Homo sapiens	Q13618 (AlphaFold model)
Kelch-like protein 22	K, L	protein	660	Homo sapiens	Q53GT1 (AlphaFold model)

Sequence of entity 1 (C, D), FASTA

>8K8T_1 Cullin-3 (chains C, D)
MSNLSKGTGSRKDTKMRIRAFPMTMDEKYVNSIWDLLKNAIQEIQRKNNSGLSFEELYRN
AYTMVLHKHGEKLYTGLREVVTEHLINKVREDVLNSLNNNFLQTLNQAWNDHQTAMVMIR
DILMYMDRVYVQQNNVENVYNLGLIIFRDQVVRYGCIRDHLRQTLLDMIARERKGEVVDR
GAIRNACQMLMILGLEGRSVYEEDFEAPFLEMSAEFFQMESQKFLAENSASVYIKKVEAR
INEEIERVMHCLDKSTEEPIVKVVERELISKHMKTIVEMENSGLVHMLKNGKTEDLGCMY
KLFSRVPNGLKTMCECMSSYLREQGKALVSEEGEGKNPVDYIQGLLDLKSRFDRFLLESF
NNDRLFKQTIAGDFEYFLNLNSRSPEYLSLFIDDKLKKGVKGLTEQEVETILDKAMVLFR
FMQEKDVFERYYKQHLARRLLTNKSVSDDSEKNMISKLKTECGCQFTSKLEGMFRDMSIS
NTTMDEFRQHLQATGVSLGGVDLTVRVLTTGYWPTQSATPKCNIPPAPRHAFEIFRRFYL
AKHSGRQLTLQHHMGSADLNATFYGPVKKEDGSEVGVGGAQVTGSNTRKHILQVSTFQMT
ILMLFNNREKYTFEEIQQETDIPERELVRALQSLACGKPTQRVLTKEPKSKEIENGHIFT
VNDQFTSKLHRVKIQTVAAKQGESDPERKETRQKVDDDRKHEIEAAIVRIMKSRKKMQHN
VLVAEVTQQLKARFLPSPVVIKKRIEGLIEREYLARTPEDRKVYTYVAKLHHHHHH

Sequence of entity 2 (K, L), FASTA

>8K8T_2 Kelch-like protein 22 (chains K, L)
MSYYHHHHHHDYDIPTTENLYFQGAMMAEEQEFTQLCKLPAQPSHPHCVNNTYRSAQHSQ
ALLRGLLALRDSGILFDVVLVVEGRHIEAHRILLAASCDYFRGMFAGGLKEMEQEEVLIH
GVSYNAMCQILHFIYTSELELSLSNVQETLVAACQLQIPEIIHFCCDFLMSWVDEENILD
VYRLAELFDLSRLTEQLDTYILKNFVAFSRTDKYRQLPLEKVYSLLSSNRLEVSCETEVY
EGALLYHYSLEQVQADQISLHEPPKLLETVRFPLMEAEVLQRLHDKLDPSPLRDTVASAL
MYHRNESLQPSLQSPQTELRSDFQCVVGFGGIHSTPSTVLSDQAKYLNPLLGEWKHFTAS
LAPRMSNQGIAVLNNFVYLIGGDNNVQGFRAESRCWRYDPRHNRWFQIQSLQQEHADLSV
CVVGRYIYAVAGRDYHNDLNAVERYDPATNSWAYVAPLKREVYAHAGATLEGKMYITCGR
RGEDYLKETHCYDPGSNTWHTLADGPVRRAWHGMATLLNKLYVIGGSNNDAGYRRDVHQV
ACYSCTSGQWSSVCPLPAGHGEPGIAVLDNRIYVLGGRSHNRGSRTGYVHIYDVEKDCWE
EGPQLDNSISGLAACVLTLPRSLLLEPPRGTPDRSQADPDFASEVMSVSDWEEFDNSSED

Primary citation

A conserved N-terminal motif of CUL3 contributes to assembly and E3 ligase activity of CRL3 KLHL22. Wang, W., Liang, L., Dai, Z. et al. Nat Commun (2024) 15:3789-3789. DOI 10.1038/s41467-024-48045-2 · PubMed

Other PDB entries of the same protein (UniProt Q13618 (AlphaFold model), which also has an AlphaFold model), best resolution first:

6I2M 2.3 Å, Crystal structure of vaccinia virus protein A55 BTB-Back domain in complex with human…
4EOZ 2.4 Å, Crystal structure of the SPOP BTB domain complexed with the Cul3 N-terminal domain
4AP2 2.8 Å, Crystal structure of the human KLHL11-Cul3 complex at 2.8A resolution
8I79 2.8 Å, Cryo-EM structure of KCTD7 in complex with Cullin3
4APF 3.1 Å, Crystal structure of the human KLHL11-Cul3 complex at 3.1A resolution
9RWZ 3.1 Å, ZSWIM8-CUL3 complex bound to AGO2-miR-7-CYRANO
9Q3E 3.3 Å, Cryo-EM structure of RotavirusA NSP1-ELOB-ELOC-CUL3
5NLB 3.45 Å, Crystal structure of human CUL3 N-terminal domain bound to KEAP1 BTB and 3-box
4HXI 3.51 Å, Crystal structure of KLHL3/Cul3 complex
8U80 3.6 Å, KCTD5/Cullin3/Gbeta1gamma2 Complex: Local Refinment of KCTD5(BTB)/Cullin3(NTD)
8KHP 3.67 Å, CULLIN3-KLHL22-RBX1 E3 ligase
8H3Q 3.76 Å, Cryo-EM Structure of the CAND1-Cul3-Rbx1 complex

Browse structure collections

About this viewer

MolViewer shows 8K8T 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.