8GHG: HSlo1 in digitonin, Ca2+-free and EDTA-free

Cryo-EM structure of hSlo1 in digitonin, Ca2+-free and EDTA-free. Determined by electron microscopy at 3.3 Å resolution. Released 10 May 2023.

Method: Electron microscopy
Resolution: 3.3 Å
Organism: Homo sapiens
Chains: 4
Atoms: 26,659
Mol. weight: 483.63 kDa
Released: 10 May 2023

Explore 8GHG in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

8GHG contains 188 α-helices and 123 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: 42 helices, 28 β-strands

Element	Residues	Length	Sheet
α-helix	22-29	8
α-helix	109-127	19
α-helix	130-134	5
α-helix	150-169	20
α-helix	174-179	6
α-helix	181-198	18
α-helix	213-215	3
α-helix	218-223	6
α-helix	230-259	30
α-helix	274-285	12
α-helix	298-318	21
α-helix	319-321	3
α-helix	323-327	5
β-strand	344-349	6	1
α-helix	353-363	11
β-strand	374-378	5	1
α-helix	382-383	2
α-helix	385-393	9
β-strand	398-400	3	1
α-helix	408-414	7
β-strand	421-425	5	1
α-helix	433-450	18
β-strand	455-458	4	1
α-helix	466-470	5
β-strand	482-483	2	1
α-helix	486-499	14
α-helix	503-508	6
α-helix	524-532	9
β-strand	535-540	6	2
β-strand	564-565	2	2
β-strand	594-599	6	2
α-helix	602-605	4
α-helix	606-608	3
β-strand	686	1	3
β-strand	692	1	4
β-strand	693	1	3
α-helix	700-703	4
β-strand	704	1	5
α-helix	707-712	6
β-strand	719-722	4	5
α-helix	730-731	2
α-helix	735-741	7
β-strand	743	1	4
α-helix	748-750	3
α-helix	751-753	3
β-strand	754-758	5	5
α-helix	760-766	7
α-helix	767-769	3
β-strand	776-780	5	5
α-helix	786-791	6
β-strand	799-802	4	5
α-helix	818-829	12
β-strand	831	1	6
β-strand	872	1	6
α-helix	873-875	3
β-strand	878-880	3	5
β-strand	881-882	2	7
α-helix	885-891	7
α-helix	910-912	3
β-strand	915-916	2	7
α-helix	917-921	5
α-helix	922-929	8
α-helix	933-941	9
α-helix	947-956	10
β-strand	975	1	8
α-helix	996-1007	12
β-strand	1010	1	8
β-strand	1014-1017	4	9
β-strand	1031-1034	4	9
β-strand	1048	1	9

Chain B: 47 helices, 30 β-strands

Element	Residues	Length	Sheet
α-helix	25-29	5
α-helix	110-132	23
α-helix	133-135	3
β-strand	140-141	2	20
α-helix	148-169	22
α-helix	174-179	6
α-helix	181-199	19
β-strand	201-202	2	20
α-helix	208-215	8
α-helix	217-223	7
α-helix	231-259	29
α-helix	262-264	3
α-helix	274-285	12
α-helix	298-318	21
α-helix	319-321	3
α-helix	323-326	4
β-strand	344-349	6	21
α-helix	353-363	11
β-strand	374-379	6	21
α-helix	382-384	3
α-helix	385-393	9
β-strand	398-402	5	21
α-helix	408-414	7
β-strand	421-425	5	21
α-helix	433-450	18
β-strand	455-458	4	21
α-helix	466-471	6
β-strand	483	1	21
α-helix	486-499	14
α-helix	503-509	7
α-helix	524-532	9
β-strand	535-540	6	22
α-helix	550-557	8
β-strand	564-568	5	22
β-strand	594-599	6	22
α-helix	602-605	4
α-helix	606-608	3
β-strand	686	1	23
β-strand	692	1	24
β-strand	693	1	23
α-helix	700-703	4
β-strand	704	1	25
α-helix	707-712	6
β-strand	719-722	4	25
α-helix	730-731	2
α-helix	735-741	7
β-strand	743	1	24
α-helix	751-753	3
β-strand	754-758	5	25
α-helix	760-766	7
α-helix	767-769	3
β-strand	776-780	5	25
α-helix	786-791	6
α-helix	794-796	3
β-strand	799-802	4	25
α-helix	805-807	3
α-helix	818-829	12
β-strand	831	1	26
β-strand	872	1	26
α-helix	873-875	3
β-strand	878-882	5	25
α-helix	885-891	7
α-helix	907-911	5
β-strand	914-916	3	25
α-helix	917-921	5
α-helix	922-929	8
α-helix	932	1
α-helix	933-937	5
α-helix	938-940	3
α-helix	949-956	8
β-strand	975-976	2	27
α-helix	996-1006	11
β-strand	1011	1	27
β-strand	1014-1017	4	28
β-strand	1031-1034	4	28
β-strand	1047	1	28
β-strand	1051-1052	2	27

Chain C: 47 helices, 32 β-strands

Element	Residues	Length	Sheet
α-helix	22-26	5
α-helix	119-135	17
α-helix	148-169	22
α-helix	176-179	4
α-helix	181-199	19
α-helix	210-213	4
α-helix	217-224	8
α-helix	233-259	27
α-helix	274-284	11
α-helix	285-287	3
α-helix	298-307	10
α-helix	308-312	5
α-helix	313-316	4
α-helix	319-326	8
β-strand	344-349	6	10
α-helix	353-363	11
β-strand	374-378	5	10
β-strand	379	1	11
α-helix	382-384	3
α-helix	385-393	9
β-strand	398-399	2	10
β-strand	402	1	11
α-helix	408-414	7
α-helix	416-418	3
β-strand	421-425	5	10
α-helix	433-450	18
β-strand	455-458	4	10
α-helix	463-465	3
α-helix	466-470	5
β-strand	482-483	2	10
α-helix	486-499	14
α-helix	503-508	6
α-helix	524-532	9
β-strand	535-538	4	12
α-helix	540-542	3
β-strand	549	1	13
α-helix	550-561	12
β-strand	564-565	2	12
β-strand	568-569	2	14
β-strand	579-580	2	14
β-strand	588	1	13
β-strand	596-599	4	12
α-helix	602-606	5
β-strand	686	1	15
β-strand	687	1	16
β-strand	692	1	17
β-strand	693	1	15
α-helix	700-702	3
β-strand	704	1	18
α-helix	707-712	6
β-strand	719-722	4	18
α-helix	734-738	5
α-helix	739-742	4
β-strand	743	1	17
α-helix	748-750	3
α-helix	751-753	3
β-strand	754-758	5	18
α-helix	760-767	8
β-strand	776-780	5	18
α-helix	786-791	6
β-strand	799-802	4	18
α-helix	818-829	12
β-strand	878-882	5	18
α-helix	885-890	6
α-helix	903-905	3
α-helix	907-911	5
β-strand	914-916	3	18
α-helix	917-920	4
α-helix	923-929	7
α-helix	933-941	9
α-helix	947-956	10
β-strand	961	1	16
α-helix	970-972	3
β-strand	976-981	6	19
α-helix	986-991	6
α-helix	996-1007	12
β-strand	1010-1017	8	19
β-strand	1031-1035	5	19
β-strand	1048-1053	6	19

Chain D: 52 helices, 33 β-strands

Element	Residues	Length	Sheet
α-helix	25-28	4
α-helix	30-32	3
α-helix	110-115	6
α-helix	119-121	3
α-helix	123-135	13
α-helix	151-170	20
α-helix	181-199	19
α-helix	208-211	4
α-helix	215-223	9
α-helix	231-235	5
α-helix	236-240	5
α-helix	241-259	19
α-helix	274-284	11
α-helix	298-317	20
α-helix	320-326	7
β-strand	343-349	7	29
α-helix	353-363	11
β-strand	373-379	7	29
α-helix	382-384	3
α-helix	385-393	9
β-strand	398-402	5	29
α-helix	408-414	7
α-helix	416-418	3
β-strand	421	1	30
β-strand	422-425	4	29
α-helix	433-450	18
β-strand	455	1	30
β-strand	458-460	3	31
α-helix	463-465	3
α-helix	466-470	5
β-strand	483-485	3	31
α-helix	486-499	14
α-helix	503-508	6
α-helix	524-532	9
β-strand	535-539	5	32
α-helix	540-542	3
β-strand	549	1	33
α-helix	550-561	12
β-strand	564-569	6	32
β-strand	579-581	3	32
β-strand	588	1	33
β-strand	595-599	5	32
α-helix	602-605	4
α-helix	606-608	3
β-strand	686	1	34
β-strand	687	1	35
β-strand	692	1	36
β-strand	693	1	34
α-helix	700-702	3
β-strand	704	1	37
α-helix	707-712	6
β-strand	719-723	5	37
α-helix	730-731	2
α-helix	734-738	5
α-helix	740-742	3
β-strand	743	1	36
α-helix	748-750	3
α-helix	751-753	3
β-strand	754-758	5	37
α-helix	760-766	7
α-helix	767-769	3
β-strand	776-780	5	37
α-helix	786-791	6
β-strand	799-802	4	37
α-helix	818-829	12
β-strand	831	1	38
β-strand	872	1	38
β-strand	879-882	4	37
α-helix	885-891	7
α-helix	903-905	3
α-helix	907-911	5
β-strand	914-916	3	37
α-helix	917-920	4
α-helix	922-929	8
α-helix	933-941	9
α-helix	947-956	10
β-strand	961	1	35
α-helix	970-973	4
β-strand	976-981	6	39
α-helix	986-988	3
α-helix	996-1007	12
β-strand	1010-1017	8	39
α-helix	1018-1020	3
β-strand	1031-1035	5	39
β-strand	1048-1053	6	39

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Calcium-activated potassium channel subunit alpha-1	A, B, C, D	protein	1072	Homo sapiens	Q12791 (AlphaFold model)

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

>8GHG_1 Calcium-activated potassium channel subunit alpha-1 (chains A, B, C, D)
MAPSRLEEELRRRLTEPDALIIPVTMEVPCDSRGQRMWWAFLASSMVTFFGGLFIILLWR
TLKYLWTVCCHCGGKTKEAQKINNGSSQADGTLKPVDEKEEAVAAEVGWMTSVKDWAGVM
ISAQTLTGRVLVVLVFALSIGALVIYFIDSSNPIESCQNFYKDFTLQIDMAFNVFFLLYF
GLRFIAANDKLWFWLEVNSVVDFFTVPPVFVSVYLNRSWLGLRFLRALRLIQFSEILQFL
NILKTSNSIKLVNLLSIFISTWLTAAGFIHLVENSGDPWENFQNNQALTYWECVYLLMVT
MSTVGYGDVYAKTTLGRLFMVFFILGGLAMFASYVPEIIELIGNRKKYGGSYSAVSGRKH
IVVCGHITLESVSNFLKDFLHKDRDDVNVEIVFLHNISPNLELEALFKRHFTQVEFYQGS
VLNPHDLARVKIESADACLILANKYCADPDAEDASNIMRVISIKNYHPKIRIITQMLQYH
NKAHLLNIPSWNWKEGDDAICLAELKLGFIAQSCLAQGLSTMLANLFSMRSFIKIEEDTW
QKYYLEGVSNEMYTEYLSSAFVGLSFPTVCELCFVKLKLLMIAIEYKSANRESRILINPG
NHLKIQEGTLGFFIASDAKEVKRAFFYCKACHDDITDPKRIKKCGCKRLEDEQPSTLSPK
KKQRNGGMRNSPNTSPKLMRHDPLLIPGNDQIDNMDSNVKKYDSTGMFHWCAPKEIEKVI
LTRSEAAMTVLSGHVVVCIFGDVSSALIGLRNLVMPLRASNFHYHELKHIVFVGSIEYLK
REWETLHNFPKVSILPGTPLSRADLRAVNINLCDMCVILSANQNNIDDTSLQDKECILAS
LNIKSMQFDDSIGVLQANSQGFTPPGMDRSSPDNSPVHGMLRQPSITTGVNIPIITELVN
DTNVQFLDQDDDDDPDTELYLTQPFACGTAFAVSVLDSLMSATYFNDNILTLIRTLVTGG
ATPELEALIAEENALRGGYSTPQTLANRDRCRVAQLALLDGPFADLGDGGCYGDLFCKAL
KTYNMLCFGIYRLRDAHLSTPSQCTKRYVITNPPYEFELVPTDLIFCLMQFD

Primary citation

Membrane protein isolation and structure determination in cell-derived membrane vesicles. Tao, X., Zhao, C., MacKinnon, R. Proc Natl Acad Sci U S A (2023) 120:e2302325120-e2302325120. DOI 10.1073/pnas.2302325120 · PubMed

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

Browse structure collections

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