4LLO: PDB entry 4LLO

Structure of the eag domain-CNBHD complex of the mouse EAG1 channel. Determined by X-ray diffraction at 2.0 Å resolution. Released 28 Aug 2013.

Method: X-ray diffraction
Resolution: 2.0 Å
Organism: Mus musculus
Chains: 8
Atoms: 9,889
Mol. weight: 142.59 kDa
Released: 28 Aug 2013

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

Secondary structure: helices and β-sheets

4LLO contains 51 α-helices and 84 β-strands across 8 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: 8 helices, 13 β-strands

Element	Residues	Length	Sheet
β-strand	555-557	3	1
α-helix	565-571	7
α-helix	573-576	4
α-helix	580-582	3
α-helix	587-596	10
β-strand	598-602	5	1
β-strand	607-609	3	2
β-strand	614-615	2	3
β-strand	617-623	7	1
β-strand	626-630	5	2
β-strand	633-638	6	2
β-strand	643-645	3	1
β-strand	655-656	2	3
β-strand	660-663	4	2
β-strand	667-673	7	1
α-helix	674-683	10
α-helix	685-694	10
β-strand	699-700	2	1
α-helix	704-705	2
β-strand	709	1	4
α-helix	710-718	9

Chain B: 5 helices, 8 β-strands

Element	Residues	Length	Sheet
α-helix	17-22	6
β-strand	29-34	6	5
β-strand	37	1	4
β-strand	41	1	6
β-strand	42-45	4	5
α-helix	47-53	7
α-helix	57-60	4
β-strand	64	1	6
α-helix	68-70	3
α-helix	77-88	12
β-strand	93-100	8	5
β-strand	106-117	12	5
β-strand	123-132	10	5

Chain C: 9 helices, 13 β-strands

Element	Residues	Length	Sheet
β-strand	556-557	2	7
α-helix	565-571	7
α-helix	573-576	4
α-helix	580-582	3
α-helix	587-596	10
β-strand	598-602	5	7
β-strand	607-609	3	8
β-strand	614-615	2	9
β-strand	617-623	7	7
β-strand	626-630	5	8
β-strand	633-638	6	8
β-strand	643-645	3	7
α-helix	654	1
β-strand	655-656	2	9
α-helix	657	1
β-strand	660-663	4	8
β-strand	667-673	7	7
α-helix	674-683	10
α-helix	685-694	10
β-strand	699-700	2	7
α-helix	704-706	3
β-strand	709	1	10

Chain D: 4 helices, 8 β-strands

Element	Residues	Length	Sheet
β-strand	29-34	6	11
β-strand	37	1	10
β-strand	41	1	12
β-strand	42-45	4	11
α-helix	47-53	7
α-helix	57-60	4
β-strand	64	1	12
α-helix	68-70	3
α-helix	77-88	12
β-strand	93-100	8	11
β-strand	106-117	12	11
β-strand	123-132	10	11

Chain E: 8 helices, 13 β-strands

Element	Residues	Length	Sheet
β-strand	556-557	2	13
α-helix	565-571	7
α-helix	573-576	4
α-helix	580-582	3
α-helix	587-596	10
β-strand	598-602	5	13
β-strand	607-609	3	14
β-strand	614-615	2	15
β-strand	617-623	7	13
β-strand	626-630	5	14
β-strand	633-638	6	14
β-strand	643-645	3	13
β-strand	655-656	2	15
β-strand	660-663	4	14
β-strand	667-673	7	13
α-helix	674-681	8
α-helix	685-694	10
β-strand	699-700	2	13
α-helix	704-706	3
β-strand	709	1	16
α-helix	710-716	7

Chain F: 5 helices, 8 β-strands

Element	Residues	Length	Sheet
α-helix	17-21	5
β-strand	29-34	6	17
β-strand	37	1	16
β-strand	41	1	18
β-strand	42-45	4	17
α-helix	47-53	7
α-helix	57-60	4
β-strand	64	1	18
α-helix	68-70	3
α-helix	77-88	12
β-strand	93-100	8	17
β-strand	106-117	12	17
β-strand	123-132	10	17

Chain G: 8 helices, 13 β-strands

Element	Residues	Length	Sheet
β-strand	556-557	2	19
α-helix	565-571	7
α-helix	573-576	4
α-helix	580-582	3
α-helix	587-594	8
β-strand	598-602	5	19
β-strand	607-609	3	20
β-strand	614-615	2	21
β-strand	617-623	7	19
β-strand	626-630	5	20
β-strand	633-638	6	20
β-strand	643-645	3	19
β-strand	655-656	2	21
β-strand	660-663	4	20
β-strand	667-673	7	19
α-helix	674-683	10
α-helix	685-694	10
β-strand	699-700	2	19
α-helix	704-706	3
β-strand	709	1	22
α-helix	710-713	4

Chain H: 4 helices, 8 β-strands

Element	Residues	Length	Sheet
β-strand	29-34	6	23
β-strand	37	1	22
β-strand	41	1	24
β-strand	42-45	4	23
α-helix	47-53	7
α-helix	57-60	4
β-strand	64	1	24
α-helix	68-70	3
α-helix	77-89	13
β-strand	93-100	8	23
β-strand	106-117	12	23
β-strand	123-132	10	23

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Potassium voltage-gated channel subfamily H member 1	A, C, E, G	protein	177	Mus musculus	Q60603 (AlphaFold model)
Potassium voltage-gated channel subfamily H member 1	B, D, F, H	protein	134	Mus musculus	Q60603 (AlphaFold model)

Sequence of entity 1 (A, C, E, G), FASTA

>4LLO_1 Potassium voltage-gated channel subfamily H member 1 (chains A, C, E, G)
GAMGTEKVLQICPKDMRADICVHLNRKVFKEHPAFRLASDGCLRALAMEFQTVHCAPGDL
IYHAGESVDSLCFVVSGSLEVIQDDEVVAILGKGDVFGDVFWKEATLAQSCANVRALTYC
DLHVIKRDALQKVLEFYTAFSHSFSRNLILTYNLRKRIVFRKISDVKREEEERMKRK

Sequence of entity 2 (B, D, F, H), FASTA

>4LLO_2 Potassium voltage-gated channel subfamily H member 1 (chains B, D, F, H)
GAMGRRGLVAPQNTFLENIVRRSNDTNFVLGNAQIVDWPIVYSNDGFCKLSGYHRAEVMQ
KSSACSFMYGELTDKDTVEKVRQTFENYEMNSFEILMYKKNRTPVWFFVKIAPIRNEQDK
VVLFLCTFSDITAF

Primary citation

The structural mechanism of KCNH-channel regulation by the eag domain. Haitin, Y., Carlson, A.E., Zagotta, W.N. Nature (2013) 501:444-448. DOI 10.1038/nature12487 · PubMed

Other PDB entries of the same protein (UniProt Q60603 (AlphaFold model), which also has an AlphaFold model), best resolution first:

4HOI 1.85 Å, Crystal structure of PAS domain from the mouse EAG1 potassium channel
4F8A 2.2 Å, Cyclic nucleotide binding-homology domain from mouse EAG1 potassium channel
5HIT 2.85 Å, Crystal Structure Analysis of Ca2+-calmodulin and a C-terminal EAG1 channel fragment

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