7YO1: RCK1 mutated human Slo1-LRRC26 complex

Cryo-EM structure of RCK1 mutated human Slo1-LRRC26 complex. Determined by electron microscopy at 3.6 Å resolution. Released 6 Mar 2024.

Method: Electron microscopy
Resolution: 3.6 Å
Organism: Homo sapiens
Chains: 8
Atoms: 35,800
Mol. weight: 617.47 kDa
Ligands: CA, MG
Released: 6 Mar 2024

Explore 7YO1 in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

7YO1 contains 229 α-helices and 167 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: 45 helices, 30 β-strands

Element	Residues	Length	Sheet
α-helix	22-47	26
α-helix	48-50	3
α-helix	94-105	12
α-helix	110-135	26
β-strand	139-140	2	1
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	1
α-helix	208-214	7
α-helix	217-223	7
α-helix	230-258	29
α-helix	262-264	3
α-helix	274-285	12
α-helix	298-327	30
β-strand	343-349	7	2
α-helix	353-363	11
β-strand	373-379	7	2
α-helix	385-393	9
β-strand	398-402	5	2
α-helix	408-413	6
β-strand	421-425	5	2
α-helix	433-450	18
β-strand	455-460	6	2
α-helix	463-470	8
β-strand	482-485	4	2
α-helix	486-499	14
α-helix	503-510	8
α-helix	524-532	9
β-strand	535-540	6	3
α-helix	541-542	2
α-helix	543-547	5
α-helix	550-559	10
β-strand	564-565	2	3
β-strand	594-599	6	3
α-helix	602-605	4
α-helix	606-608	3
β-strand	686-687	2	4
β-strand	692	1	5
β-strand	693	1	4
α-helix	700-703	4
β-strand	704	1	6
α-helix	707-712	6
β-strand	718-724	7	6
α-helix	734-738	5
β-strand	743	1	5
α-helix	751-753	3
β-strand	754-757	4	6
α-helix	760-766	7
α-helix	767-769	3
β-strand	776-779	4	6
α-helix	786-791	6
β-strand	797-804	8	6
α-helix	819-828	10
β-strand	831	1	7
β-strand	872	1	7
α-helix	873-875	3
β-strand	878-881	4	6
α-helix	885-890	6
α-helix	907-910	4
β-strand	914-915	2	6
α-helix	917-919	3
α-helix	922-929	8
α-helix	931-941	11
α-helix	947-956	10
β-strand	961-962	2	4
α-helix	966-972	7
β-strand	975-981	7	8
α-helix	988-992	5
α-helix	996-1007	12
β-strand	1010	1	8
β-strand	1013-1017	5	8
β-strand	1031-1035	5	8
β-strand	1047-1054	8	8

Chain B: 6 helices, 10 β-strands

Element	Residues	Length	Sheet
α-helix	66	1
β-strand	76-79	4	9
β-strand	85	1	10
β-strand	99-103	5	9
β-strand	109	1	10
β-strand	123-126	4	9
β-strand	147-151	5	9
α-helix	160-163	4
β-strand	171-175	5	9
α-helix	184-188	5
β-strand	195-197	3	9
β-strand	204	1	11
α-helix	209-218	10
β-strand	232	1	11
α-helix	259-265	7
α-helix	268-300	33

Chain C: 50 helices, 29 β-strands

Element	Residues	Length	Sheet
α-helix	22-47	26
α-helix	94-105	12
α-helix	110-134	25
β-strand	139-140	2	12
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	12
α-helix	208-214	7
α-helix	217-224	8
α-helix	230-258	29
α-helix	262-264	3
α-helix	274-285	12
α-helix	298-327	30
β-strand	343-348	6	13
α-helix	353-363	11
α-helix	369-370	2
β-strand	373-379	7	13
α-helix	385-393	9
β-strand	398-402	5	13
α-helix	408-413	6
β-strand	421-424	4	13
α-helix	433-450	18
β-strand	455-460	6	13
α-helix	463-470	8
α-helix	477-479	3
β-strand	482-485	4	13
α-helix	486-499	14
α-helix	503-510	8
α-helix	524-532	9
β-strand	535-540	6	14
α-helix	543-547	5
α-helix	550-556	7
α-helix	557-561	5
β-strand	564-565	2	14
β-strand	594-599	6	14
α-helix	602-607	6
β-strand	686-687	2	15
β-strand	692	1	16
β-strand	693	1	15
α-helix	696-699	4
α-helix	700-703	4
β-strand	704	1	17
α-helix	707-712	6
β-strand	719-724	6	17
α-helix	730-732	3
α-helix	735-738	4
β-strand	743	1	16
α-helix	751-753	3
β-strand	754-757	4	17
α-helix	760-763	4
α-helix	767-769	3
β-strand	776-779	4	17
α-helix	786-791	6
α-helix	794-796	3
β-strand	799-804	6	17
α-helix	818-828	11
β-strand	831	1	18
β-strand	872	1	18
α-helix	873-875	3
β-strand	878-882	5	17
α-helix	885-890	6
α-helix	903-905	3
α-helix	907-910	4
β-strand	914-916	3	17
α-helix	917-920	4
α-helix	921-929	9
α-helix	931-938	8
α-helix	939-943	5
α-helix	947-955	9
β-strand	961-962	2	15
α-helix	966-971	6
β-strand	974-981	8	19
α-helix	988-990	3
α-helix	996-1006	11
β-strand	1013-1017	5	19
β-strand	1031-1035	5	19
β-strand	1047-1055	9	19

Chain D: 12 helices, 11 β-strands

Element	Residues	Length	Sheet
α-helix	56-57	2
α-helix	65-66	2
β-strand	76-79	4	20
β-strand	85	1	21
α-helix	86-87	2
α-helix	90-93	4
β-strand	100-103	4	20
β-strand	109	1	21
α-helix	112-115	4
β-strand	123-127	5	20
β-strand	147-151	5	20
α-helix	160-163	4
β-strand	171-175	5	20
α-helix	184-189	6
β-strand	195-197	3	20
β-strand	204	1	22
α-helix	207-209	3
α-helix	210-218	9
α-helix	221-223	3
α-helix	225-227	3
β-strand	231-232	2	22
β-strand	239-240	2	22
α-helix	262-300	39

Chain E: 49 helices, 29 β-strands

Element	Residues	Length	Sheet
α-helix	23-47	25
α-helix	48-50	3
α-helix	94-105	12
α-helix	110-134	25
β-strand	139-141	3	23
α-helix	148-170	23
α-helix	174-178	5
α-helix	181-187	7
α-helix	190-199	10
β-strand	201-203	3	23
α-helix	207-214	8
α-helix	217-223	7
α-helix	230-258	29
α-helix	262-264	3
α-helix	274-285	12
α-helix	298-327	30
β-strand	343-348	6	24
α-helix	353-363	11
β-strand	373-378	6	24
α-helix	385-393	9
β-strand	398-401	4	24
α-helix	408-413	6
α-helix	416-418	3
β-strand	421-424	4	24
α-helix	433-450	18
β-strand	455-460	6	24
α-helix	463-470	8
α-helix	477-479	3
β-strand	482-485	4	24
α-helix	486-499	14
α-helix	503-511	9
α-helix	524-532	9
β-strand	535-540	6	25
α-helix	541-542	2
α-helix	543-547	5
α-helix	550-559	10
β-strand	564-565	2	25
β-strand	594-599	6	25
α-helix	602-609	8
β-strand	686-687	2	26
β-strand	692	1	27
β-strand	693	1	26
α-helix	696-699	4
α-helix	700-703	4
β-strand	704	1	28
α-helix	707-712	6
β-strand	718-724	7	28
α-helix	735-738	4
β-strand	743	1	27
α-helix	751-753	3
β-strand	754-758	5	28
α-helix	760-766	7
α-helix	767-769	3
β-strand	776-780	5	28
α-helix	786-791	6
β-strand	797-804	8	28
α-helix	818-829	12
β-strand	831	1	29
β-strand	872	1	29
α-helix	873-875	3
β-strand	878-882	5	28
α-helix	885-890	6
α-helix	896-897	2
α-helix	903-905	3
α-helix	907-910	4
β-strand	914-916	3	28
α-helix	917-920	4
α-helix	922-929	8
α-helix	931-941	11
α-helix	947-956	10
β-strand	961-962	2	26
α-helix	966-972	7
β-strand	974-981	8	30
α-helix	996-1002	7
α-helix	1003-1007	5
β-strand	1011-1017	7	30
β-strand	1031-1035	5	30
β-strand	1047-1055	9	30

Chain F: 10 helices, 15 β-strands

Element	Residues	Length	Sheet
α-helix	48-50	3
β-strand	54	1	31
α-helix	56-57	2
β-strand	73	1	31
β-strand	77-79	3	32
β-strand	85-86	2	33
β-strand	99-103	5	32
β-strand	109-110	2	33
β-strand	123-125	3	32
α-helix	134-135	2
β-strand	147	1	32
β-strand	150-151	2	34
α-helix	160-163	4
β-strand	171-173	3	32
β-strand	174-175	2	34
α-helix	184-189	6
β-strand	195-197	3	32
β-strand	203-204	2	35
α-helix	209-218	10
α-helix	225-227	3
β-strand	230-232	3	35
β-strand	240-241	2	35
α-helix	246	1
α-helix	260-265	6
α-helix	268-300	33

Chain G: 48 helices, 32 β-strands

Element	Residues	Length	Sheet
α-helix	22-47	26
α-helix	48-50	3
α-helix	94-105	12
α-helix	110-135	26
β-strand	139-140	2	36
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	36
α-helix	208-214	7
α-helix	217-223	7
α-helix	230-258	29
α-helix	262-264	3
α-helix	274-285	12
α-helix	299-326	28
β-strand	339	1	37
β-strand	342	1	37
β-strand	343-349	7	38
α-helix	353-363	11
β-strand	373-379	7	38
α-helix	385-393	9
β-strand	398-402	5	38
α-helix	408-413	6
β-strand	421-425	5	38
α-helix	433-450	18
β-strand	456-460	5	38
α-helix	463-470	8
β-strand	482-485	4	38
α-helix	486-499	14
α-helix	503-510	8
α-helix	524-532	9
β-strand	535-540	6	39
α-helix	543-547	5
α-helix	550-556	7
α-helix	557-561	5
β-strand	564-565	2	39
α-helix	578-580	3
β-strand	594-599	6	39
α-helix	602-606	5
β-strand	686	1	40
β-strand	687	1	41
β-strand	692	1	42
β-strand	693	1	40
α-helix	700-702	3
β-strand	704	1	43
α-helix	707-712	6
β-strand	718-724	7	43
α-helix	730-731	2
α-helix	735-738	4
β-strand	743	1	42
α-helix	751-753	3
β-strand	754-758	5	43
α-helix	760-766	7
α-helix	767-769	3
β-strand	776-780	5	43
α-helix	786-791	6
β-strand	797-804	8	43
α-helix	813-815	3
α-helix	818-828	11
β-strand	831	1	44
β-strand	872	1	44
α-helix	873-875	3
β-strand	878-882	5	43
α-helix	885-890	6
α-helix	903-905	3
α-helix	907-910	4
β-strand	914-916	3	43
α-helix	917-919	3
α-helix	923-929	7
α-helix	931-941	11
α-helix	947-955	9
β-strand	961	1	41
α-helix	966-972	7
β-strand	975-981	7	45
α-helix	988-990	3
α-helix	996-1006	11
β-strand	1013-1017	5	45
β-strand	1031-1035	5	45
β-strand	1047-1054	8	45

Chain H: 9 helices, 11 β-strands

Element	Residues	Length	Sheet
α-helix	48-50	3
α-helix	65-67	3
β-strand	76-79	4	46
β-strand	85-86	2	47
α-helix	87	1
β-strand	99-103	5	46
β-strand	109-110	2	47
β-strand	123-127	5	46
β-strand	147-151	5	46
α-helix	160-163	4
β-strand	171-175	5	46
α-helix	184-189	6
β-strand	196-199	4	46
β-strand	203-204	2	48
α-helix	207-209	3
α-helix	210-218	9
β-strand	230-232	3	48
β-strand	240-241	2	48
α-helix	259-265	7
α-helix	268-301	34

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

>7YO1_1 Calcium-activated potassium channel subunit alpha-1 (chains A, C, E, G)
MDALIIPVTMEVPCDSRGQRMWWAFLASSMVTFFGGLFIILLWRTLKYLWTVCCHCGGKT
KEAQKINNGSSQADGTLKPVDEKEEAVAAEVGWMTSVKDWAGVMISAQTLTGRVLVVLVF
ALSIGALVIYFIDSSNPIESCQNFYKDFTLQIDMAFNVFFLLYFGLRFIAANDKLWFWLE
VNSVVDFFTVPPVFVSVYLNRSWLGLRFLRALRLIQFSEILQFLNILKTSNSIKLVNLLS
IFISTWLTAAGFIHLVENSGDPWENFQNNQALTYWECVYLLMVTMSTVGYGDVYAKTTLG
RLFMVFFILGGLAMFASYVPEIIELIGNRKKYGGSYSAVSGRKHIVVCGHITLESVSNFL
KAFLHKARDDVNVEIVFLHNISPNLELEALFKRHFTQVEFYQGSVLNPHDLARVKIESAD
ACLILANKYCADPDAEDASNIMRVISIKNYHPKIRIITQMLQYHNKAHLLNIPSWNWKEG
DDAICLAELKLGFIAQSCLAQGLSTMLANLFSMRSFIKIEEDTWQKYYLEGVSNEMYTEY
LSSAFVGLSFPTVCELCFVKLKLLMIAIEYKSANRESRSRSRILINPGNHLKIQEGTLGF
FIASDAKEVKRAFFYCKACHDDITDPKRIKKCGCKRLEDEQPSTLSPKKKQRNGGMRNSP
NTSPKLMRHDPLLIPGNDQIDNMDSNVKKYDSTGMFHWCAPKEIEKVILTRSEAAMTVLS
GHVVVCIFGDVSSALIGLRNLVMPLRASNFHYHELKHIVFVGSIEYLKREWETLHNFPKV
SILPGTPLSRADLRAVNINLCDMCVILSANQNNIDDTSLQDKECILASLNIKSMQFDDSI
GVLQANSQGFTPPGMDRSSPDNSPVHGMLRQPSITTGVNIPIITELVNDTNVQFLDQDDD
DDPDTELYLTQPFACGTAFAVSVLDSLMSATYFNDNILTLIRTLVTGGATPELEALIAEE
NALRGGYSTPQTLANRDRCRVAQLALLDGPFADLGDGGCYGDLFCKALKTYNMLCFGIYR
LRDAHLSTPSQCTKRYVITNPPYEFELVPTDLIFCLMQFD

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

>7YO1_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
CA	Calcium ion	Ca	8
MG	Magnesium ion	Mg	4

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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