7YNZ: Human Slo1-LRRC26 complex with C1 symmetry

Cryo-EM structure of human Slo1-LRRC26 complex with C1 symmetry. Determined by electron microscopy at 3.5 Å resolution. Released 6 Mar 2024.

Method: Electron microscopy
Resolution: 3.5 Å
Organism: Homo sapiens
Chains: 8
Atoms: 35,844
Mol. weight: 617.83 kDa
Ligands: MG, CA
Released: 6 Mar 2024

Explore 7YNZ in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

7YNZ contains 226 α-helices and 159 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: 48 helices, 29 β-strands

Element	Residues	Length	Sheet
α-helix	22-48	27
α-helix	93-105	13
α-helix	110-133	24
β-strand	139-141	3	1
α-helix	149-170	22
α-helix	174-178	5
α-helix	181-187	7
α-helix	190-199	10
β-strand	201-203	3	1
α-helix	206-214	9
α-helix	218-223	6
α-helix	230-258	29
α-helix	262-264	3
α-helix	274-285	12
α-helix	298-326	29
β-strand	344-349	6	2
α-helix	353-363	11
β-strand	374-379	6	2
α-helix	382-383	2
α-helix	385-393	9
β-strand	398-402	5	2
α-helix	408-413	6
α-helix	416-418	3
β-strand	422-425	4	2
α-helix	433-450	18
β-strand	456-458	3	2
β-strand	459-460	2	3
α-helix	463-470	8
β-strand	484-485	2	3
α-helix	486-499	14
α-helix	503-509	7
α-helix	524-532	9
β-strand	537-540	4	4
α-helix	541-542	2
α-helix	550-554	5
α-helix	558-561	4
β-strand	565	1	4
β-strand	594-597	4	4
β-strand	686	1	5
β-strand	692	1	6
β-strand	693	1	5
α-helix	700-702	3
β-strand	704	1	7
α-helix	707-712	6
β-strand	719-724	6	7
α-helix	735-738	4
α-helix	739-741	3
β-strand	743	1	6
α-helix	751-753	3
β-strand	754-758	5	7
α-helix	760-765	6
β-strand	776-779	4	7
α-helix	786-791	6
α-helix	794-796	3
β-strand	799-804	6	7
α-helix	806-808	3
α-helix	818-829	12
β-strand	831	1	8
β-strand	872	1	8
α-helix	873-875	3
β-strand	878-881	4	7
α-helix	885-887	3
α-helix	888-891	4
α-helix	903-905	3
α-helix	907-910	4
β-strand	914-915	2	7
α-helix	917-919	3
α-helix	923-929	7
α-helix	932-940	9
α-helix	946-955	10
α-helix	966-970	5
β-strand	976-980	5	9
α-helix	986-988	3
α-helix	996-1007	12
β-strand	1013-1017	5	9
β-strand	1031-1035	5	9
β-strand	1047-1053	7	9

Chain B: 10 helices, 12 β-strands

Element	Residues	Length	Sheet
β-strand	48-50	3	10
β-strand	54-56	3	10
β-strand	75-77	3	10
β-strand	85-86	2	11
β-strand	99-101	3	10
β-strand	109-110	2	11
β-strand	123-125	3	10
β-strand	147-149	3	10
α-helix	160-163	4
β-strand	171-173	3	10
α-helix	182-183	2
α-helix	187-189	3
β-strand	195-197	3	10
α-helix	207-209	3
α-helix	210-218	9
α-helix	223-226	4
β-strand	230	1	12
β-strand	241	1	12
α-helix	242-244	3
α-helix	248-250	3
α-helix	255-257	3
α-helix	260-296	37

Chain C: 46 helices, 28 β-strands

Element	Residues	Length	Sheet
α-helix	22-48	27
α-helix	93-105	13
α-helix	110-133	24
β-strand	139-141	3	13
α-helix	149-170	22
α-helix	174-178	5
α-helix	181-187	7
α-helix	190-199	10
β-strand	201-203	3	13
α-helix	206-214	9
α-helix	218-223	6
α-helix	230-258	29
α-helix	262-264	3
α-helix	274-285	12
α-helix	298-326	29
α-helix	338-339	2
β-strand	343-349	7	14
α-helix	353-363	11
β-strand	373-379	7	14
α-helix	382-383	2
α-helix	385-392	8
β-strand	398-402	5	14
α-helix	408-413	6
α-helix	416-418	3
β-strand	422-425	4	14
α-helix	433-450	18
β-strand	456-460	5	14
α-helix	463-470	8
β-strand	482-485	4	14
α-helix	486-499	14
α-helix	503-511	9
α-helix	524-532	9
β-strand	537-540	4	15
α-helix	550-554	5
α-helix	558-561	4
β-strand	565	1	15
β-strand	594-597	4	15
β-strand	686	1	16
β-strand	692	1	17
β-strand	693	1	16
α-helix	700-702	3
β-strand	704	1	18
α-helix	707-712	6
β-strand	719-724	6	18
α-helix	735-738	4
α-helix	739-741	3
β-strand	743	1	17
α-helix	751-753	3
β-strand	754-758	5	18
α-helix	760-765	6
β-strand	776-780	5	18
α-helix	786-791	6
β-strand	799-804	6	18
α-helix	806-808	3
α-helix	818-829	12
β-strand	831	1	19
β-strand	872	1	19
α-helix	873-875	3
β-strand	878-881	4	18
α-helix	885-889	5
α-helix	903-905	3
α-helix	907-910	4
β-strand	914-915	2	18
α-helix	917-920	4
α-helix	922-929	8
α-helix	932-938	7
α-helix	947-956	10
α-helix	971-973	3
β-strand	976-981	6	20
α-helix	988-993	6
α-helix	996-1007	12
β-strand	1013-1017	5	20
β-strand	1031-1035	5	20
β-strand	1047-1053	7	20

Chain D: 11 helices, 12 β-strands

Element	Residues	Length	Sheet
β-strand	48-50	3	21
β-strand	54-56	3	21
β-strand	75-77	3	21
β-strand	85-86	2	22
β-strand	99-101	3	21
β-strand	109-110	2	22
β-strand	123-125	3	21
β-strand	147-149	3	21
α-helix	160-163	4
β-strand	171-173	3	21
α-helix	182-183	2
α-helix	187-189	3
β-strand	195-197	3	21
α-helix	207-209	3
α-helix	210-218	9
α-helix	220-222	3
α-helix	223-226	4
β-strand	230	1	23
β-strand	241	1	23
α-helix	242-244	3
α-helix	248-250	3
α-helix	255-257	3
α-helix	260-297	38

Chain E: 46 helices, 28 β-strands

Element	Residues	Length	Sheet
α-helix	22-48	27
α-helix	93-105	13
α-helix	110-133	24
β-strand	139-140	2	24
α-helix	148-170	23
α-helix	174-178	5
α-helix	181-187	7
α-helix	190-199	10
β-strand	202-203	2	24
α-helix	206-214	9
α-helix	218-223	6
α-helix	230-258	29
α-helix	262-264	3
α-helix	274-285	12
α-helix	298-326	29
β-strand	344-349	6	25
α-helix	353-363	11
α-helix	369-370	2
β-strand	374-379	6	25
α-helix	382-383	2
α-helix	385-393	9
β-strand	398-402	5	25
α-helix	408-413	6
β-strand	421-425	5	25
α-helix	433-450	18
β-strand	455-460	6	25
α-helix	463-470	8
β-strand	482-485	4	25
α-helix	486-499	14
α-helix	503-511	9
α-helix	524-532	9
β-strand	537-540	4	26
α-helix	544-546	3
α-helix	550-554	5
α-helix	557-561	5
β-strand	565	1	26
β-strand	594-597	4	26
α-helix	602-605	4
β-strand	686	1	27
β-strand	687	1	28
β-strand	693	1	27
α-helix	700-703	4
β-strand	704	1	29
α-helix	707-712	6
β-strand	719-724	6	29
α-helix	730-731	2
α-helix	735-738	4
α-helix	751-753	3
β-strand	754-758	5	29
α-helix	760-770	11
β-strand	776-780	5	29
α-helix	786-791	6
β-strand	799-804	6	29
α-helix	818-829	12
β-strand	831	1	30
β-strand	872	1	30
α-helix	873-875	3
β-strand	878-881	4	29
α-helix	888-891	4
α-helix	903-905	3
α-helix	907-910	4
β-strand	914-915	2	29
α-helix	919-922	4
α-helix	923-929	7
α-helix	931-940	10
α-helix	947-956	10
β-strand	961	1	28
α-helix	966-970	5
β-strand	976-981	6	31
α-helix	987-993	7
α-helix	996-1007	12
β-strand	1013-1017	5	31
β-strand	1031-1035	5	31
β-strand	1047-1053	7	31

Chain F: 11 helices, 12 β-strands

Element	Residues	Length	Sheet
β-strand	48-50	3	32
β-strand	54-56	3	32
β-strand	75-77	3	32
β-strand	85-86	2	33
β-strand	99-101	3	32
β-strand	109-110	2	33
β-strand	123-125	3	32
β-strand	147-149	3	32
α-helix	160-163	4
β-strand	171-173	3	32
α-helix	182-183	2
α-helix	187-189	3
β-strand	195-197	3	32
α-helix	207-209	3
α-helix	210-218	9
α-helix	220-222	3
α-helix	223-228	6
β-strand	230	1	34
β-strand	241	1	34
α-helix	242-244	3
α-helix	248-250	3
α-helix	255-257	3
α-helix	260-297	38

Chain G: 44 helices, 28 β-strands

Element	Residues	Length	Sheet
α-helix	22-48	27
α-helix	93-105	13
α-helix	110-133	24
β-strand	139-140	2	35
α-helix	148-170	23
α-helix	174-178	5
α-helix	181-187	7
α-helix	190-199	10
β-strand	202-203	2	35
α-helix	206-214	9
α-helix	218-223	6
α-helix	230-258	29
α-helix	262-264	3
α-helix	274-285	12
α-helix	298-326	29
β-strand	343-349	7	36
α-helix	353-363	11
β-strand	373-379	7	36
α-helix	382-383	2
α-helix	385-393	9
β-strand	398-402	5	36
α-helix	408-413	6
β-strand	422-425	4	36
α-helix	433-450	18
β-strand	456-460	5	36
α-helix	463-470	8
β-strand	482-485	4	36
α-helix	486-499	14
α-helix	503-511	9
α-helix	524-532	9
β-strand	537-540	4	37
α-helix	544-546	3
α-helix	550-554	5
α-helix	558-561	4
β-strand	565	1	37
β-strand	594-597	4	37
α-helix	602-605	4
β-strand	686	1	38
β-strand	692	1	39
β-strand	693	1	38
α-helix	700-703	4
β-strand	704	1	40
α-helix	707-712	6
β-strand	719-724	6	40
α-helix	729-731	3
α-helix	735-741	7
β-strand	743	1	39
β-strand	754-758	5	40
α-helix	760-765	6
β-strand	776-780	5	40
α-helix	786-791	6
α-helix	794-796	3
β-strand	799-804	6	40
α-helix	818-829	12
β-strand	831	1	41
β-strand	872	1	41
α-helix	873-875	3
β-strand	878-881	4	40
α-helix	885-890	6
α-helix	907-910	4
β-strand	914-915	2	40
α-helix	917-920	4
α-helix	921-929	9
α-helix	931-940	10
α-helix	947-956	10
α-helix	966-970	5
β-strand	976-981	6	42
α-helix	988-993	6
α-helix	996-1006	11
β-strand	1010-1017	8	42
β-strand	1031-1035	5	42
β-strand	1047-1053	7	42

Chain H: 10 helices, 10 β-strands

Element	Residues	Length	Sheet
β-strand	48-50	3	43
β-strand	54-56	3	43
β-strand	75-77	3	43
β-strand	85-86	2	44
β-strand	99-101	3	43
β-strand	109-110	2	44
β-strand	123-125	3	43
β-strand	147-149	3	43
α-helix	160-163	4
β-strand	171-173	3	43
α-helix	182-183	2
β-strand	195-197	3	43
α-helix	207-209	3
α-helix	210-218	9
α-helix	220-222	3
α-helix	223-226	4
α-helix	242-244	3
α-helix	248-250	3
α-helix	255-257	3
α-helix	260-297	38

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Calcium-activated potassium channel subunit alpha-1	A, C, E, G	protein	1060	Homo sapiens	Q12791 (AlphaFold model)
Leucine-rich repeat-containing protein 26	B, D, F, H	protein	334	Homo sapiens	Q2I0M4 (AlphaFold model)

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

>7YNZ_1 Calcium-activated potassium channel subunit alpha-1 (chains A, C, E, G)
MDALIIPVTMEVPCDSRGQRMWWAFLASSMVTFFGGLFIILLWRTLKYLWTVCCHCGGKT
KEAQKINNGSSQADGTLKPVDEKEEAVAAEVGWMTSVKDWAGVMISAQTLTGRVLVVLVF
ALSIGALVIYFIDSSNPIESCQNFYKDFTLQIDMAFNVFFLLYFGLRFIAANDKLWFWLE
VNSVVDFFTVPPVFVSVYLNRSWLGLRFLRALRLIQFSEILQFLNILKTSNSIKLVNLLS
IFISTWLTAAGFIHLVENSGDPWENFQNNQALTYWECVYLLMVTMSTVGYGDVYAKTTLG
RLFMVFFILGGLAMFASYVPEIIELIGNRKKYGGSYSAVSGRKHIVVCGHITLESVSNFL
KDFLHKDRDDVNVEIVFLHNISPNLELEALFKRHFTQVEFYQGSVLNPHDLARVKIESAD
ACLILANKYCADPDAEDASNIMRVISIKNYHPKIRIITQMLQYHNKAHLLNIPSWNWKEG
DDAICLAELKLGFIAQSCLAQGLSTMLANLFSMRSFIKIEEDTWQKYYLEGVSNEMYTEY
LSSAFVGLSFPTVCELCFVKLKLLMIAIEYKSANRESRSRSRILINPGNHLKIQEGTLGF
FIASDAKEVKRAFFYCKACHDDITDPKRIKKCGCKRLEDEQPSTLSPKKKQRNGGMRNSP
NTSPKLMRHDPLLIPGNDQIDNMDSNVKKYDSTGMFHWCAPKEIEKVILTRSEAAMTVLS
GHVVVCIFGDVSSALIGLRNLVMPLRASNFHYHELKHIVFVGSIEYLKREWETLHNFPKV
SILPGTPLSRADLRAVNINLCDMCVILSANQNNIDDTSLQDKECILASLNIKSMQFDDSI
GVLQANSQGFTPPGMDRSSPDNSPVHGMLRQPSITTGVNIPIITELVNDTNVQFLDQDDD
DDPDTELYLTQPFACGTAFAVSVLDSLMSATYFNDNILTLIRTLVTGGATPELEALIAEE
NALRGGYSTPQTLANRDRCRVAQLALLDGPFADLGDGGCYGDLFCKALKTYNMLCFGIYR
LRDAHLSTPSQCTKRYVITNPPYEFELVPTDLIFCLMQFD

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

>7YNZ_2 Leucine-rich repeat-containing protein 26 (chains B, D, F, H)
MRGPSWSRPRPLLLLLLLLSPWPVWAQVSATASPSGSLGAPDCPEVCTCVPGGLASCSAL
SLPAVPPGLSLRLRALLLDHNRVRALPPGAFAGAGALQRLDLRENGLHSVHVRAFWGLGA
LQLLDLSANQLEALAPGTFAPLRALRNLSLAGNRLARLEPAALGALPLLRSLSLQDNELA
ALAPGLLGRLPALDALHLRGNPWGCGCALRPLCAWLRRHPLPASEAETVLCVWPGRLTLS
PLTAFSDAAFSHCAQPLALRDLAVVYTLGPASFLVSLASCLALGSGLTACRARRRRLRTA
ALRPPRPPDPNPDPDPHGCASPADPGSPAAAAQA

Ligands and cofactors

ID	Name	Formula	Copies
MG	Magnesium ion	Mg	4
CA	Calcium ion	Ca	8

Primary citation

Structural basis for dual allosteric gating modulation of Slo1-LRRC channel complex. Yamanouchi, D. To be published.

Other PDB entries of the same protein (UniProt Q12791 (AlphaFold model), which also has an AlphaFold model), best resolution first:

6V5A 2.0 Å, Crystal structure of the human BK channel gating ring L390P mutant
8V60 2.43 Å, F315A mutant of human Slo1 in presence of EDTA - resting VSD
11DA 2.57 Å, Human Slo1-PenitremA complex under divalent chelated condition - full model
9CZM 2.57 Å, Ca2+ bound open-inactivated hSlo1 + beta2N-beta4 channel in nanodisc.
11DC 2.58 Å, Human Slo1-PenitremA complex under divalent chelated condition - gating-ring masked out
11CZ 2.6 Å, Human Slo1-paxilline complex under divalent chelated condition - full model
8V64 2.6 Å, RCK1-RCK2 double mutant of human Slo1 in presence of EDTA - resting VSD
8GHF 2.7 Å, cryo-EM structure of hSlo1 in plasma membrane vesicles
11DB 2.71 Å, Human Slo1-Paxilline complex under divalent chelated condition - gating-ring masked
8V63 2.72 Å, R207A mutant of human Slo1 in presence of EDTA - activated VSD
9JO3 2.8 Å, Cryo-EM structure of human BKca channel-compound 10b complex
8VAZ 2.82 Å, Structure of human Slo1 and human LRRC26 in EDTA - LRRD masked

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