7YO2: RCK1-RCK2 mutated human Slo1 apo

Cryo-EM structure of RCK1-RCK2 mutated human Slo1 apo. Determined by electron microscopy at 3.3 Å resolution. Released 6 Mar 2024.

Method: Electron microscopy
Resolution: 3.3 Å
Organism: Homo sapiens
Chains: 4
Atoms: 27,884
Mol. weight: 475.51 kDa
Released: 6 Mar 2024

Explore 7YO2 in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

7YO2 contains 201 α-helices and 128 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 A: 50 helices, 32 β-strands

Element	Residues	Length	Sheet
α-helix	22-33	12
α-helix	94-103	10
α-helix	110-135	26
β-strand	139	1	1
α-helix	148-170	23
α-helix	174-178	5
α-helix	181-198	18
β-strand	203	1	1
α-helix	207-214	8
α-helix	216-223	8
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	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	464-471	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	543-545	3
β-strand	549	1	4
α-helix	550-559	10
β-strand	564-570	7	3
β-strand	578-581	4	3
β-strand	588	1	4
β-strand	594-599	6	3
α-helix	602-609	8
β-strand	686-687	2	5
β-strand	693	1	5
α-helix	700-703	4
β-strand	704	1	6
α-helix	707-712	6
β-strand	719-723	5	6
α-helix	730-732	3
α-helix	735-738	4
α-helix	748-750	3
α-helix	751-753	3
β-strand	754-758	5	6
α-helix	760-763	4
α-helix	767-770	4
β-strand	776-780	5	6
α-helix	786-791	6
β-strand	799-803	5	6
α-helix	813-816	4
α-helix	818-828	11
β-strand	831	1	7
β-strand	872	1	7
α-helix	873-875	3
β-strand	878-882	5	6
α-helix	885-891	7
α-helix	903-905	3
α-helix	907-910	4
β-strand	914-916	3	6
α-helix	919-929	11
α-helix	931-942	12
α-helix	947-956	10
α-helix	959-960	2
β-strand	961-962	2	5
α-helix	966-969	4
α-helix	970-972	3
β-strand	976-981	6	8
α-helix	988-991	4
β-strand	995	1	9
α-helix	996-1007	12
β-strand	1010-1017	8	8
β-strand	1031-1035	5	8
α-helix	1041	1
β-strand	1042	1	9
α-helix	1043	1
β-strand	1047-1053	7	8
α-helix	1054-1055	2

Chain B: 50 helices, 32 β-strands

Element	Residues	Length	Sheet
α-helix	22-33	12
α-helix	94-103	10
α-helix	110-134	25
β-strand	139	1	10
α-helix	148-170	23
α-helix	174-178	5
α-helix	181-199	19
β-strand	203	1	10
α-helix	206-212	7
α-helix	216-223	8
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	11
α-helix	353-363	11
β-strand	373-379	7	11
α-helix	385-393	9
β-strand	398-402	5	11
α-helix	408-413	6
β-strand	421-425	5	11
α-helix	433-450	18
β-strand	455-460	6	11
α-helix	464-471	8
β-strand	482-485	4	11
α-helix	486-499	14
α-helix	503-511	9
α-helix	524-532	9
β-strand	535-540	6	12
α-helix	541-542	2
α-helix	543-545	3
β-strand	549	1	13
α-helix	550-556	7
α-helix	557-561	5
β-strand	564-570	7	12
β-strand	578-581	4	12
β-strand	588	1	13
β-strand	594-599	6	12
α-helix	602-607	6
β-strand	686-687	2	14
β-strand	693	1	14
α-helix	700-702	3
β-strand	704	1	15
α-helix	707-712	6
β-strand	719-723	5	15
α-helix	735-741	7
α-helix	748-750	3
α-helix	751-753	3
β-strand	754-758	5	15
α-helix	760-763	4
α-helix	767-770	4
β-strand	776-780	5	15
α-helix	786-791	6
α-helix	794-796	3
β-strand	799-803	5	15
α-helix	814-816	3
α-helix	818-828	11
β-strand	831	1	16
β-strand	872	1	16
α-helix	873-875	3
β-strand	878-882	5	15
α-helix	885-891	7
α-helix	903-905	3
α-helix	907-910	4
β-strand	914-916	3	15
α-helix	919-929	11
α-helix	931-941	11
α-helix	947-956	10
β-strand	961-962	2	14
α-helix	966-970	5
β-strand	976-981	6	17
α-helix	988-991	4
β-strand	995	1	18
α-helix	996-1007	12
β-strand	1010-1017	8	17
β-strand	1031-1035	5	17
α-helix	1041	1
β-strand	1042	1	18
α-helix	1043	1
β-strand	1047-1053	7	17
α-helix	1054-1055	2

Chain C: 52 helices, 32 β-strands

Element	Residues	Length	Sheet
α-helix	22-33	12
α-helix	94-105	12
α-helix	110-134	25
β-strand	139	1	19
α-helix	148-170	23
α-helix	174-177	4
α-helix	181-199	19
β-strand	203	1	19
α-helix	207-212	6
α-helix	216-223	8
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	20
α-helix	353-363	11
β-strand	374-378	5	20
α-helix	385-393	9
β-strand	398-401	4	20
α-helix	408-413	6
β-strand	421-425	5	20
α-helix	433-450	18
β-strand	455-460	6	20
α-helix	464-470	7
α-helix	477-479	3
β-strand	482-485	4	20
α-helix	486-499	14
α-helix	503-511	9
α-helix	524-532	9
β-strand	535-540	6	21
α-helix	541-542	2
α-helix	543-545	3
β-strand	549	1	22
α-helix	550-556	7
α-helix	557-561	5
β-strand	564-570	7	21
β-strand	578-581	4	21
β-strand	588	1	22
β-strand	594-599	6	21
α-helix	602-605	4
α-helix	606-608	3
β-strand	686-687	2	23
β-strand	693	1	23
α-helix	700-703	4
β-strand	704	1	24
α-helix	707-712	6
β-strand	719-723	5	24
α-helix	735-738	4
α-helix	739-741	3
α-helix	751-753	3
β-strand	754-758	5	24
α-helix	760-766	7
α-helix	767-769	3
β-strand	776-780	5	24
α-helix	786-791	6
α-helix	794-796	3
β-strand	799-803	5	24
α-helix	813-816	4
α-helix	818-828	11
β-strand	831	1	25
β-strand	872	1	25
α-helix	873-875	3
β-strand	878-882	5	24
α-helix	888-891	4
α-helix	903-905	3
α-helix	907-910	4
β-strand	914-916	3	24
α-helix	919-929	11
α-helix	931-941	11
α-helix	947-956	10
β-strand	961-962	2	23
α-helix	966-969	4
α-helix	970-972	3
β-strand	976-981	6	26
α-helix	988-991	4
β-strand	995	1	27
α-helix	996-1007	12
β-strand	1010-1017	8	26
β-strand	1031-1035	5	26
α-helix	1041	1
β-strand	1042	1	27
α-helix	1043	1
β-strand	1047-1053	7	26
α-helix	1054-1055	2

Chain D: 49 helices, 32 β-strands

Element	Residues	Length	Sheet
α-helix	22-33	12
α-helix	94-103	10
α-helix	110-134	25
β-strand	139	1	28
α-helix	148-170	23
α-helix	174-177	4
α-helix	181-198	18
β-strand	203	1	28
α-helix	206-214	9
α-helix	216-223	8
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	29
α-helix	353-363	11
β-strand	374-378	5	29
α-helix	385-393	9
β-strand	398-401	4	29
α-helix	408-413	6
β-strand	421-425	5	29
α-helix	433-450	18
β-strand	456-460	5	29
α-helix	464-471	8
β-strand	482-485	4	29
α-helix	486-499	14
α-helix	503-510	8
α-helix	524-532	9
β-strand	535-540	6	30
α-helix	541-542	2
α-helix	543-545	3
β-strand	549	1	31
α-helix	550-559	10
β-strand	564-570	7	30
β-strand	578-581	4	30
β-strand	588	1	31
β-strand	594-599	6	30
α-helix	602-609	8
β-strand	686-687	2	32
β-strand	693	1	32
α-helix	700-703	4
β-strand	704	1	33
α-helix	707-712	6
β-strand	719-723	5	33
α-helix	730-732	3
α-helix	735-738	4
α-helix	748-750	3
α-helix	751-753	3
β-strand	754-758	5	33
α-helix	760-770	11
β-strand	776-780	5	33
α-helix	786-791	6
α-helix	794-796	3
β-strand	799-803	5	33
α-helix	813-816	4
α-helix	818-828	11
β-strand	831	1	34
β-strand	872	1	34
α-helix	873-875	3
β-strand	878-882	5	33
α-helix	885-891	7
α-helix	903-905	3
α-helix	907-910	4
β-strand	914-916	3	33
α-helix	919-929	11
α-helix	931-941	11
α-helix	947-956	10
β-strand	961-962	2	32
α-helix	966-969	4
α-helix	970-972	3
β-strand	976-981	6	35
α-helix	988-991	4
β-strand	995	1	36
α-helix	996-1006	11
β-strand	1010-1017	8	35
β-strand	1031-1035	5	35
α-helix	1041	1
β-strand	1042	1	36
α-helix	1043	1
β-strand	1047-1053	7	35
α-helix	1054-1055	2

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Calcium-activated potassium channel subunit alpha-1	A, B, C, D	protein	1056	Homo sapiens	Q12791 (AlphaFold model)

Sequence of entity 1 (A, B, C, D), FASTA

>7YO2_1 Calcium-activated potassium channel subunit alpha-1 (chains A, B, C, D)
MDALIIPVTMEVPCDSRGQRMWWAFLASSMVTFFGGLFIILLWRTLKYLWTVCCHCGGKT
KEAQKINNGSSQADGTLKPVDEKEEAVAAEVGWMTSVKDWAGVMISAQTLTGRVLVVLVF
ALSIGALVIYFIDSSNPIESCQNFYKDFTLQIDMAFNVFFLLYFGLRFIAANDKLWFWLE
VNSVVDFFTVPPVFVSVYLNRSWLGLRFLRALRLIQFSEILQFLNILKTSNSIKLVNLLS
IFISTWLTAAGFIHLVENSGDPWENFQNNQALTYWECVYLLMVTMSTVGYGDVYAKTTLG
RLFMVFFILGGLAMFASYVPEIIELIGNRKKYGGSYSAVSGRKHIVVCGHITLESVSNFL
KAFLHKARDDVNVEIVFLHNISPNLELEALFKRHFTQVEFYQGSVLNPHDLARVKIESAD
ACLILANKYCADPDAEDASNIMRVISIKNYHPKIRIITQMLQYHNKAHLLNIPSWNWKEG
DDAICLAELKLGFIAQSCLAQGLSTMLANLFSMRSFIKIEEDTWQKYYLEGVSNEMYTEY
LSSAFVGLSFPTVCELCFVKLKLLMIAIEYKSANRESRILINPGNHLKIQEGTLGFFIAS
DAKEVKRAFFYCKACHDDITDPKRIKKCGCKRLEDEQPSTLSPKKKQRNGGMRNSPNTSP
KLMRHDPLLIPGNDQIDNMDSNVKKYDSTGMFHWCAPKEIEKVILTRSEAAMTVLSGHVV
VCIFGDVSSALIGLRNLVMPLRASNFHYHELKHIVFVGSIEYLKREWETLHNFPKVSILP
GTPLSRADLRAVNINLCDMCVILSANQNNIDDTSLQDKECILASLNIKSMQFDDSIGVLQ
ANSQGFTPPGMDRSSPDNSPVHGMLRQPSITTGVNIPIITELVNDTNVQFLDQNNNNNPD
TELYLTQPFACGTAFAVSVLDSLMSATYFNDNILTLIRTLVTGGATPELEALIAEENALR
GGYSTPQTLANRDRCRVAQLALLDGPFADLGDGGCYGDLFCKALKTYNMLCFGIYRLRDA
HLSTPSQCTKRYVITNPPYEFELVPTDLIFCLMQFD

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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