9EJK: Lgl2

Lgl2 bound to the aPKCiota-Par6b complex in nucleotide-free form. Head sub-complex region subtracted. Determined by electron microscopy at 3.08 Å resolution. Released 2 Jul 2025.

Method: Electron microscopy
Resolution: 3.08 Å
Organisms: Homo sapiens, Mus musculus
Chains: 3
Atoms: 9,854
Mol. weight: 220.35 kDa
Released: 2 Jul 2025

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

Secondary structure: helices and β-sheets

9EJK contains 36 α-helices and 99 β-strands across 3 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: 20 helices, 74 β-strands

Element	Residues	Length	Sheet
α-helix	14-20	7
β-strand	21-27	7	1
β-strand	30	1	2
α-helix	31-32	2
β-strand	35-41	7	3
β-strand	46-51	6	3
β-strand	55-59	5	3
β-strand	65-69	5	3
β-strand	76-81	6	4
α-helix	82	1
β-strand	87-92	6	4
β-strand	96-102	7	4
β-strand	105	1	5
β-strand	108	1	5
β-strand	111-118	8	4
α-helix	127-130	4
β-strand	132-137	6	6
β-strand	143-148	6	6
β-strand	153-157	5	6
β-strand	163-169	7	6
α-helix	171-176	6
α-helix	180-182	3
β-strand	191-196	6	7
β-strand	203-208	6	7
β-strand	212-217	6	7
β-strand	223-228	6	7
α-helix	232	1
β-strand	233-238	6	8
β-strand	244-249	6	8
β-strand	254-258	5	8
β-strand	270-272	3	8
β-strand	280	1	9
β-strand	285-289	5	10
β-strand	297-301	5	10
β-strand	305	1	9
β-strand	313-318	6	10
β-strand	323-328	6	10
β-strand	334-338	5	11
β-strand	352-356	5	11
β-strand	361-365	5	11
β-strand	373	1	11
β-strand	387-394	8	12
α-helix	398-409	12
α-helix	419-420	2
β-strand	426-427	2	13
α-helix	429-432	4
β-strand	436-442	7	12
β-strand	446-451	6	12
β-strand	458-464	7	12
β-strand	469	1	14
β-strand	490-492	3	10
β-strand	499-500	2	15
α-helix	503-505	3
β-strand	507-513	7	16
β-strand	518-523	6	16
β-strand	527-534	8	16
β-strand	538-540	3	17
α-helix	541-542	2
β-strand	543-548	6	16
β-strand	566	1	14
α-helix	567-568	2
β-strand	571-573	3	17
β-strand	576-586	11	16
β-strand	593-597	5	18
β-strand	602-606	5	18
β-strand	610-615	6	18
β-strand	620-626	7	18
α-helix	634-636	3
β-strand	651	1	19
β-strand	697-699	3	20
β-strand	713-721	9	21
β-strand	730-737	8	21
β-strand	741-748	8	21
α-helix	752-754	3
β-strand	761-769	9	21
α-helix	774-775	2
β-strand	776-781	6	22
α-helix	788-791	4
α-helix	794-797	4
β-strand	810-815	6	22
β-strand	818-823	6	22
β-strand	829-834	6	22
α-helix	836-839	4
β-strand	843-852	10	23
β-strand	860-868	9	23
β-strand	872-877	6	23
β-strand	883-888	6	23
α-helix	896-899	4
β-strand	902-903	2	1
β-strand	908-910	3	1
β-strand	912-914	3	2
β-strand	917-918	2	2
β-strand	920-924	5	1
β-strand	933-934	2	13

Chain B: 13 helices, 16 β-strands

Element	Residues	Length	Sheet
α-helix	251-253	3
β-strand	254-262	9	24
β-strand	266-273	8	24
β-strand	278-286	9	24
α-helix	298-308	11
β-strand	315	1	25
β-strand	320-323	4	24
β-strand	327-333	7	24
β-strand	339	1	25
α-helix	340-347	8
α-helix	352-371	20
β-strand	375	1	26
β-strand	384-386	3	25
β-strand	392-394	3	25
β-strand	401	1	26
β-strand	410	1	27
β-strand	414	1	19
α-helix	417-419	3
α-helix	422-426	5
β-strand	430	1	27
α-helix	433-448	16
α-helix	467-476	10
β-strand	481-482	2	15
α-helix	487-496	10
α-helix	512-517	6
α-helix	527-531	5
α-helix	546-551	6
α-helix	554-557	4
β-strand	584-585	2	24

Chain C: 3 helices, 9 β-strands

Element	Residues	Length	Sheet
β-strand	156-160	5	20
β-strand	171-180	10	20
β-strand	187-197	11	20
α-helix	202-206	5
α-helix	213	1
β-strand	214-218	5	20
β-strand	221-222	2	20
α-helix	228-237	10
β-strand	242-247	6	20
β-strand	296-299	4	21
β-strand	305-306	2	21
β-strand	309	1	22

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
LLGL scribble cell polarity complex component 2	A	protein	980	Homo sapiens	Q6P1M3 (AlphaFold model)
Protein kinase C iota type	B	protein	596	Homo sapiens	P41743 (AlphaFold model)
Partitioning defective 6 homolog beta	C	protein	383	Mus musculus	Q9JK83 (AlphaFold model)

Sequence of entity 1 (A), FASTA

>9EJK_1 LLGL scribble cell polarity complex component 2 (chains A)
MRERLKRDLFQFNKTVEHGFPHQPSALGYSPSLRILAIGTRSGAIKLYGAPGVEFMGLHQ
ENNAVTQIHLLPGQCQLVTLLDDNSLHLWSLKVKGGASELQEDESFTLRGPPGAAPSATQ
ITVVLPHSSCELLYLGTESGNVFVVQLPAFRALEDRTISSDAVLQRLPEEARHRRVFEMV
EALQEHPRDPNQILIGYSRGLVVIWDLQGSRVLYHFLSSQQLENIWWQRDGRLLVSCHSD
GSYCQWPVSSEAQQPEPLRSLVPYGPFPCKAITRILWLTTRQGLPFTIFQGGMPRASYGD
RHCISVIHDGQQTAFDFTSRVIGFTVLTEADPAATFDDPYALVVLAEEELVVIDLQTAGW
PPVQLPYLASLHCSAITCSHHVSNIPLKLWERIIAAGSRQNAHFSTMEWPIDGGTSLTPA
PPQRDLLLTGHEDGTVRFWDASGVCLRLLYKLSTVRVFLTDTDPNENFSAQGEDEWPPLR
KVGSFDPYSDDPRLGIQKIFLCKYSGYLAVAGTAGQVLVLELNDEAAEQAVEQVEADLLQ
DQEGYRWKGHERLAARSGPVRFEPGFQPFVLVQCQPPAVVTSLALHSEWRLVAFGTSHGF
GLFDHQQRRQVFVKCTLHPSDQLALEGPLSRVKSLKKSLRQSFRRMRRSRVSSRKRHPAG
PPGEAQEGSAKAERPGLQNMELAPVQRKIEARSAEDSFTGFVRTLYFADTYLKDSSRHCP
SLWAGTNGGTIYAFSLRVPPAERRMDEPVRAEQAKEIQLMHRAPVVGILVLDGHSVPLPE
PLEVAHDLSKSPDMQGSHQLLVVSEEQFKVFTLPKVSAKLKLKLTALEGSRVRRVSVAHF
GSRRAEDYGEHHLAVLTNLGDIQVVSLPLLKPQVRYSCIRREDVSGIASCVFTKYGQGFY
LISPSEFERFSLSTKWLVEPRCLVDSAETKNHRPGNGAGPKKAPSRARNSGTQSDGEEKQ
PGLVMEREFTTSASENLYFQ

Sequence of entity 2 (B), FASTA

>9EJK_2 Protein kinase C iota type (chains B)
MPTQRDSSTMSHTVAGGGSGDHSHQVRVKAYYRGDIMITHFEPSISFEGLCNEVRDMCSF
DNEQLFTMKWIDEEGDPCTVSSQLELEEAFRLYELNKDSELLIHVFPCVPERPGMPCPGE
DKSIYRRGARRWRKLYCANGHTFQAKRFNRRAHCAICTDRIWGLGRQGYKCINCKLLVHK
KCHKLVTIECGRHSLPQEPVMPMDQSSMHSDHAQTVIPYNPSSHESLDQVGEEKEAMNTR
ESGKASSSLGLQDFDLLRVIGRGSYAKVLLVRLKKTDRIYAMKVVKKELVNDDEDIDWVQ
TEKHVFEQASNHPFLVGLHSCFQTESRLFFVIEYVNGGDLMFHMQRQRKLPEEHARFYSA
EISLALNYLHERGIIYRDLKLDNVLLDSEGHIKLTDYGMCKEGLRPGDTTSTFCGTPNYI
APEILRGEDYGFSVDWWALGVLMFEMMAGRSPFDIVGSSDNPDQNTEDYLFQVILEKQIR
IPRSLSVKAASVLKSFLNKDPKERLGCHPQTGFADIQGHPFFRNVDWDMMEQKQVVPPFK
PNISGEFGLDNFDSQFTNEPVQLTPDDDDIVRKIDQSEFEGFEYINPLLMSAEECV

Sequence of entity 3 (C), FASTA

>9EJK_3 Partitioning defective 6 homolog beta (chains C)
MNRGHRHGASSGCLGTMEVKSKFGAEFRRFSLERSKPGKFEEFYGLLQHVHKIPNVDVLV
GYADIHGDLPPINNDDNYHKAVSTANPLLRIFIQKKEEADYSAFGTDTLIRKKNMLSNVL
RPDNHRKKPHIVISMPQDFRPVSSIIDVDILPETHRRVRLCKYGTEKPLGFYIRDGSSVR
VTPHGLEKVPGIFISRLVPGGLAQSTGLLAVNDEVLEVNGIEVSGKSLDQVTDMMIANSR
NLIITVRPANQRNNVVRNSRTSGSSSQSTDNSLLGFPQQVEASFEPEDQDSDEDDIIIED
SGEPQQIPKATPAQSLESLTQIELSFESGQNGFSPPQDTSLVPVPGSLDTELESRAPDQK
LLEEDGTIITLEFTTASENLYFQ

Primary citation

Polarity protein Par6 facilitates the processive phosphorylation of Lgl via a dynamic interaction with aPKC. Almagor, L., Weis, W.I. Commun Biol (2025) 8:967-967. DOI 10.1038/s42003-025-08401-4 · PubMed

Other PDB entries of the same protein (UniProt Q6P1M3 (AlphaFold model), which also has an AlphaFold model), best resolution first:

6N8R 1.91 Å, Crystal structure of the human cell polarity protein Lethal Giant Larvae 2 (Lgl2). aPKC…
3WP0 2.04 Å, Crystal structure of Dlg GK in complex with a phosphor-Lgl2 peptide
6N8Q 2.2 Å, Crystal structure of the human cell polarity protein Lethal Giant Larvae 2 (Lgl2).…
8R3X 2.59 Å, Crystal structure of aPKC Iota kinase domain with LLGL2 peptide
3WP1 2.8 Å, Phosphorylation-dependent interaction between tumor suppressors Dlg and Lgl
6N8P 3.19 Å, Crystal structure of the human cell polarity protein Lethal Giant Larvae 2 (Lgl2).…
9EJM 3.33 Å, Lgl2 bound to the aPKCiota-Par6B complex in its ADP-bound form
9EJL 3.48 Å, Lgl2 bound to the aPKCiota-Par6B complex in nucleotide-free form. Conformation with…
6N8S 3.9 Å, Crystal structure of the human cell polarity protein Lethal Giant Larvae 2 (Lgl2). aPKC…

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