6V22: Ca2+-bound hsSlo1-beta4 channel complex

Cryo-EM structure of Ca2+-bound hsSlo1-beta4 channel complex. Determined by electron microscopy at 3.2 Å resolution. Released 25 Dec 2019.

Method: Electron microscopy
Resolution: 3.2 Å
Organism: Homo sapiens
Chains: 8
Atoms: 37,004
Mol. weight: 634.05 kDa
Ligands: CA, POV, NAG, CLR
Released: 25 Dec 2019

Explore 6V22 in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

6V22 contains 204 α-helices and 188 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.

Chains A, B, C and D: 44 helices, 38 β-strands

Element	Residues	Length	Sheet
α-helix	22-46	25
α-helix	94-105	12
α-helix	110-133	24
β-strand	139-141	3	1
α-helix	148-170	23
α-helix	174-178	5
α-helix	181-199	19
β-strand	201-203	3	1
α-helix	207-216	10
α-helix	217-222	6
α-helix	230-258	29
α-helix	262-264	3
α-helix	274-285	12
α-helix	298-325	28
β-strand	339	1	2
β-strand	342	1	2
β-strand	344-349	6	3
α-helix	353-363	11
β-strand	374-379	6	3
α-helix	382-383	2
α-helix	385-393	9
β-strand	398-402	5	3
α-helix	408-413	6
β-strand	421-425	5	3
α-helix	433-450	18
β-strand	456-460	5	3
α-helix	464-470	7
β-strand	482-485	4	3
α-helix	486-499	14
α-helix	503-509	7
α-helix	524-532	9
β-strand	535-540	6	4
α-helix	543-545	3
β-strand	549	1	5
α-helix	550-556	7
α-helix	557-561	5
β-strand	564-568	5	4
β-strand	581	1	4
β-strand	588	1	5
β-strand	594-599	6	4
α-helix	605-608	4
β-strand	686-687	2	6
β-strand	692	1	7
β-strand	693	1	6
α-helix	700-702	3
β-strand	704	1	8
α-helix	707-712	6
β-strand	719-724	6	8
α-helix	730-731	2
α-helix	735-738	4
α-helix	739-742	4
β-strand	743	1	7
β-strand	754-758	5	8
α-helix	760-770	11
β-strand	776-780	5	8
α-helix	786-791	6
β-strand	799-804	6	8
α-helix	818-828	11
β-strand	831	1	9
β-strand	872	1	9
β-strand	878-882	5	8
α-helix	885-890	6
α-helix	903-905	3
α-helix	907-910	4
β-strand	914-916	3	8
α-helix	917-922	6
α-helix	923-929	7
α-helix	932-941	10
α-helix	947-955	9
β-strand	961-962	2	6
α-helix	966-970	5
α-helix	971-973	3
β-strand	976-981	6	10
α-helix	988-991	4
β-strand	994-995	2	11
α-helix	996-1006	11
β-strand	1010-1014	5	10
β-strand	1017	1	12
β-strand	1031	1	12
β-strand	1034-1035	2	10
β-strand	1042-1043	2	11
β-strand	1048-1053	6	10

Chains E, F, G and H: 7 helices, 9 β-strands

Element	Residues	Length	Sheet
α-helix	2012-2035	24
α-helix	2036-2040	5
α-helix	2041-2048	8
β-strand	2050-2061	12	13
β-strand	2066-2067	2	14
β-strand	2070	1	15
β-strand	2078	1	15
β-strand	2081-2082	2	14
β-strand	2085-2091	7	13
β-strand	2097-2101	5	13
α-helix	2104-2109	6
α-helix	2117-2119	3
α-helix	2123-2139	17
β-strand	2146-2151	6	13
β-strand	2155-2160	6	13
α-helix	2169-2203	35

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Calcium-activated potassium channel subunit alpha-1	A, B, C, D	protein	1065	Homo sapiens	Q12791 (AlphaFold model)
Calcium-activated potassium channel subunit beta-4	E, F, G, H	protein	219	Homo sapiens	Q86W47 (AlphaFold model)

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

>6V22_1 Calcium-activated potassium channel subunit alpha-1 (chains A, B, C, D)
MDALIIPVTMEVPCDSRGQRMWWAFLASSMVTFFGGLFIILLWRTLKYLWTVCCHCGGKT
KEAQKINNGSSQADGTLKPVDEKEEAVAAEVGWMTSVKDWAGVMISAQTLTGRVLVVLVF
ALSIGALVIYFIDSSNPIESCQNFYKDFTLQIDMAFNVFFLLYFGLRFIAANDKLWFWLE
VNSVVDFFTVPPVFVSVYLNRSWLGLRFLRALRLIQFSEILQFLNILKTSNSIKLVNLLS
IFISTWLTAAGFIHLVENSGDPWENFQNNQALTYWECVYLLMVTMSTVGYGDVYAKTTLG
RLFMVFFILGGLAMFASYVPEIIELIGNRKKYGGSYSAVSGRKHIVVCGHITLESVSNFL
KDFLHKDRDDVNVEIVFLHNISPNLELEALFKRHFTQVEFYQGSVLNPHDLARVKIESAD
ACLILANKYCADPDAEDASNIMRVISIKNYHPKIRIITQMLQYHNKAHLLNIPSWNWKEG
DDAICLAELKLGFIAQSCLAQGLSTMLANLFSMRSFIKIEEDTWQKYYLEGVSNEMYTEY
LSSAFVGLSFPTVCELCFVKLKLLMIAIEYKSANRESRILINPGNHLKIQEGTLGFFIAS
DAKEVKRAFFYCKACHDDITDPKRIKKCGCKRLEDEQPSTLSPKKKQRNGGMRNSPNTSP
KLMRHDPLLIPGNDQIDNMDSNVKKYDSTGMFHWCAPKEIEKVILTRSEAAMTVLSGHVV
VCIFGDVSSALIGLRNLVMPLRASNFHYHELKHIVFVGSIEYLKREWETLHNFPKVSILP
GTPLSRADLRAVNINLCDMCVILSANQNNIDDTSLQDKECILASLNIKSMQFDDSIGVLQ
ANSQGFTPPGMDRSSPDNSPVHGMLRQPSITTGVNIPIITELVNDTNVQFLDQDDDDDPD
TELYLTQPFACGTAFAVSVLDSLMSATYFNDNILTLIRTLVTGGATPELEALIAEENALR
GGYSTPQTLANRDRCRVAQLALLDGPFADLGDGGCYGDLFCKALKTYNMLCFGIYRLRDA
HLSTPSQCTKRYVITNPPYEFELVPTDLIFCLMQFDSNSLEVLFQ

Sequence of entity 2 (E, F, G, H), FASTA

>6V22_2 Calcium-activated potassium channel subunit beta-4 (chains E, F, G, H)
MAKLRVAYEYTEAEDKSIRLGLFLIISGVVSLFIFGFCWLSPALQDLQATEANCTVLSVQ
QIGEVFECTFTCGADCRGTSQYPCVQVYVNNSESNSRALLHSDEHQLLTNPKCSYIPPCK
RENQKNLESVMNWQQYWKDEIGSQPFTCYFNQHQRPDDVLLHRTHDEIVLLHCFLWPLVT
FVVGVLIVVLTICAKSLAVKAEAMKKRKFSSNSLEVLFQ

Ligands and cofactors

ID	Name	Formula	Copies
CA	Calcium ion	Ca	8
POV	(2S)-3-(hexadecanoyloxy)-2-[(9Z)-octadec-9-enoyloxy]propyl…	C42 H82 N O8 P	60
NAG	2-acetamido-2-deoxy-beta-D-glucopyranose	C8 H15 N O6	8
CLR	Cholesterol	C27 H46 O	16
MG	Magnesium ion	Mg	4

Water and common crystallization additives (K) are not listed.

Primary citation

Molecular structures of the human Slo1 K + channel in complex with beta 4. Tao, X., MacKinnon, R. Elife (2019) 8. DOI 10.7554/eLife.51409 · 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

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