6V35: Ca2+-free hsSlo1-beta4 channel complex

Cryo-EM structure of Ca2+-free hsSlo1-beta4 channel complex. Determined by electron microscopy at 3.5 Å resolution. Released 25 Dec 2019.

Method: Electron microscopy
Resolution: 3.5 Å
Organism: Homo sapiens
Chains: 8
Atoms: 36,488
Mol. weight: 614.74 kDa
Ligands: NAG, CLR, PGW
Released: 25 Dec 2019

Explore 6V35 in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

6V35 contains 244 α-helices and 176 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: 51 helices, 37 β-strands

Element	Residues	Length	Sheet
α-helix	23-46	24
α-helix	97-100	4
α-helix	102-105	4
α-helix	110-133	24
β-strand	141	1	1
α-helix	149-166	18
α-helix	174-179	6
α-helix	190-199	10
β-strand	201	1	1
α-helix	208-216	9
α-helix	217-223	7
α-helix	230-258	29
α-helix	262-264	3
α-helix	274-285	12
α-helix	298-316	19
α-helix	323-325	3
β-strand	343-349	7	2
α-helix	353-363	11
α-helix	366-368	3
β-strand	373-379	7	2
α-helix	382-383	2
α-helix	385-391	7
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	464-466	3
α-helix	467-471	5
β-strand	482-485	4	2
α-helix	486-499	14
α-helix	503-511	9
α-helix	524-528	5
β-strand	535-540	6	3
α-helix	541-542	2
α-helix	543-545	3
β-strand	549	1	4
α-helix	550-560	11
β-strand	564-567	4	3
β-strand	569-570	2	5
β-strand	578-579	2	5
β-strand	588	1	4
α-helix	589-590	2
α-helix	593	1
β-strand	594-599	6	3
α-helix	602-606	5
α-helix	622-624	3
β-strand	686	1	6
β-strand	687	1	7
β-strand	693	1	6
α-helix	700-703	4
β-strand	704	1	8
α-helix	707-712	6
β-strand	719-722	4	8
α-helix	730-731	2
α-helix	735-741	7
β-strand	754-758	5	8
α-helix	760-766	7
α-helix	767-769	3
β-strand	776-780	5	8
α-helix	786-790	5
β-strand	799-802	4	8
α-helix	813-815	3
α-helix	818-828	11
β-strand	831	1	9
β-strand	872	1	9
α-helix	873-875	3
β-strand	878-882	5	8
α-helix	885-890	6
α-helix	907-910	4
β-strand	914-916	3	8
α-helix	918-929	12
α-helix	933-941	9
α-helix	947-956	10
β-strand	961	1	7
α-helix	966-971	6
β-strand	978-981	4	10
α-helix	986-991	6
α-helix	996-1007	12
β-strand	1013	1	10
β-strand	1014	1	11
β-strand	1016	1	12
β-strand	1017	1	13
α-helix	1018-1020	3
β-strand	1031	1	13
β-strand	1034	1	11
β-strand	1047	1	12
β-strand	1048-1051	4	10

Chains E, F, G and H: 10 helices, 7 β-strands

Element	Residues	Length	Sheet
α-helix	2009-2011	3
α-helix	2012-2035	24
α-helix	2040-2046	7
β-strand	2050-2061	12	14
β-strand	2066-2067	2	15
β-strand	2081-2082	2	15
β-strand	2085-2090	6	14
β-strand	2097-2101	5	14
α-helix	2104-2109	6
α-helix	2116-2119	4
α-helix	2123-2138	16
α-helix	2145	1
β-strand	2146-2150	5	14
β-strand	2158-2160	3	14
α-helix	2167-2170	4
α-helix	2171-2199	29
α-helix	2201-2203	3

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

>6V35_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

>6V35_2 Calcium-activated potassium channel subunit beta-4 (chains E, F, G, H)
MAKLRVAYEYTEAEDKSIRLGLFLIISGVVSLFIFGFCWLSPALQDLQATEANCTVLSVQ
QIGEVFECTFTCGADCRGTSQYPCVQVYVNNSESNSRALLHSDEHQLLTNPKCSYIPPCK
RENQKNLESVMNWQQYWKDEIGSQPFTCYFNQHQRPDDVLLHRTHDEIVLLHCFLWPLVT
FVVGVLIVVLTICAKSLAVKAEAMKKRKFSSNSLEVLFQ

Ligands and cofactors

ID	Name	Formula	Copies
NAG	2-acetamido-2-deoxy-beta-D-glucopyranose	C8 H15 N O6	8
CLR	Cholesterol	C27 H46 O	8
PGW	(1R)-2-{[(S)-{[(2S)-2,3-dihydroxypropyl]oxy}(hydroxy)phosphoryl]oxy}-1-[(hexade…	C40 H77 O10 P	40

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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