9CHS: PDB entry 9CHS

Cryo-EM structure of the human ether-a-go-go related K+ channel (hERG) in 3 mM K+ without symmetry. Determined by electron microscopy at 3.4 Å resolution. Released 21 Aug 2024.

Method: Electron microscopy
Resolution: 3.4 Å
Organism: Homo sapiens
Chains: 4
Atoms: 9,508
Mol. weight: 350.73 kDa
Released: 21 Aug 2024

Explore 9CHS in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

9CHS contains 69 α-helices and 24 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: 16 helices, 6 β-strands

Element	Residues	Length	Sheet
β-strand	400	1	1
α-helix	405-431	27
α-helix	453-470	18
β-strand	473	1	1
β-strand	475-476	2	2
β-strand	482-483	2	2
α-helix	486-495	10
α-helix	498-503	6
α-helix	518-524	7
α-helix	525-531	7
α-helix	532-537	6
α-helix	539-542	4
α-helix	546-575	30
α-helix	585-592	8
α-helix	596	1
β-strand	597	1	3
α-helix	598	1
β-strand	603	1	3
α-helix	607-622	16
α-helix	635-666	32
α-helix	668-687	20
α-helix	691-708	18

Chain B: 17 helices, 6 β-strands

Element	Residues	Length	Sheet
β-strand	400	1	4
α-helix	405-431	27
α-helix	451-470	20
β-strand	473	1	4
β-strand	475-476	2	5
β-strand	482-483	2	5
α-helix	486-494	9
α-helix	498-503	6
α-helix	508-510	3
α-helix	518-524	7
α-helix	525-532	8
α-helix	533-537	5
α-helix	539-542	4
α-helix	546-573	28
α-helix	585-592	8
α-helix	596	1
β-strand	597	1	6
α-helix	598	1
β-strand	603	1	6
α-helix	607-622	16
α-helix	635-666	32
α-helix	668-686	19
α-helix	691-708	18

Chain C: 18 helices, 6 β-strands

Element	Residues	Length	Sheet
β-strand	400	1	7
α-helix	405-427	23
α-helix	428-432	5
α-helix	451-470	20
β-strand	473	1	7
β-strand	475-476	2	8
β-strand	482-483	2	8
α-helix	486-494	9
α-helix	498-503	6
α-helix	508-510	3
α-helix	518-524	7
α-helix	525-532	8
α-helix	533-536	4
α-helix	539-542	4
α-helix	546-573	28
α-helix	585-592	8
α-helix	596	1
β-strand	597	1	9
α-helix	598	1
β-strand	603	1	9
α-helix	607-622	16
α-helix	635-666	32
α-helix	668-687	20
α-helix	691-708	18

Chain D: 18 helices, 6 β-strands

Element	Residues	Length	Sheet
β-strand	400	1	10
α-helix	405-431	27
α-helix	451-470	20
β-strand	473	1	10
β-strand	475-476	2	11
β-strand	482-483	2	11
α-helix	486-494	9
α-helix	498-503	6
α-helix	508-510	3
α-helix	518-524	7
α-helix	525-532	8
α-helix	533-536	4
α-helix	539-542	4
α-helix	546-573	28
α-helix	585-592	8
α-helix	596	1
β-strand	597	1	12
α-helix	598	1
β-strand	603	1	12
α-helix	607-622	16
α-helix	635-652	18
α-helix	655-666	12
α-helix	668-687	20
α-helix	691-708	18

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Potassium voltage-gated channel subfamily H member 2	A, B, C, D	protein	784	Homo sapiens	Q12809 (AlphaFold model)

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

>9CHS_1 Potassium voltage-gated channel subfamily H member 2 (chains A, B, C, D)
MPVRRGHVAPQNTFLDTIIRKFEGQSRKFIIANARVENCAVIYCNDGFCELCGYSRAEVM
QRPCTCDFLHGPRTQRRAAAQIAQALLGAEERKVEIAFYRKDGSCFLCLVDVVPVKNEDG
AVIMFILNFEVVMEKDMVGSGADVLPEYKLQAPRIHRWTILHYSPFKAVWDWLILLLVIY
TAVFTPYSAAFLLKETEEGPPATECGYACQPLAVVDLIVDIMFIVDILINFRTTYVNANE
EVVSHPGRIAVHYFKGWFLIDMVAAIPFDLLIFGSGSEELIGLLKTARLLRLVRVARKLD
RYSEYGAAVLFLLMCTFALIAHWLACIWYAIGNMEQPHMDSRIGWLHNLGDQIGKPYNSS
GLGGPSIKDKYVTALYFTFSSLTSVGFGNVSPNTNSEKIFSICVMLIGSLMYASIFGNVS
AIIQRLYSGTARYHTQMLRVREFIRFHQIPNPLRQRLEEYFQHAWSYTNGIDMNAVLKGF
PECLQADICLHLNRSLLQHCKPFRGATKGCLRALAMKFKTTHAPPGDTLVHAGDLLTALY
FISRGSIEILRGDVVVAILGKNDIFGEPLNLYARPGKSNGDVRALTYCDLHKIHRDDLLE
VLDMYPEFSDHFWSSLEITFNLRDTNMIPGGRQYQELPRCPAPTPSLLNIPLSSPGRRPR
GDVESRLDALQRQLNRLETRLSADMATVLQLLQRQMTLVPPAYSAVTTPGPGPTSTSPLL
PVSPLPTLTLDSLSQVSQFMACEELPPGAPELPQEGPTRRLSLPGQLGALTSQPLHRHGS
DPGS

Primary citation

Potassium dependent structural changes in the selectivity filter of HERG potassium channels. Lau, C.H.Y., Flood, E., Hunter, M.J. et al. Nat Commun (2024) 15:7470-7470. DOI 10.1038/s41467-024-51208-w · PubMed

Other PDB entries of the same protein (UniProt Q12809 (AlphaFold model), which also has an AlphaFold model), best resolution first:

4HQA 1.96 Å, Crystal structure of PAS domain from the human ERG (hERG) potassium channel
4HP9 2.12 Å, Crystal structure of the N-terminal truncated PAS domain from the hERG potassium channel
1BYW 2.6 Å, Structure of the N-terminal domain of the human-erg potassium channel
9CHQ 3.0 Å, Cryo-EM structure of the human ether-a-go-go related K+ channel (hERG) in 3 mM K+
8ZYQ 3.18 Å, Cryo-EM Structure of pimozide-bound hERG Channel
8ZYP 3.19 Å, Cryo-EM Structure of E-4031-bound hERG Channel
8ZYN 3.27 Å, Cryo-EM Structure of inhibitor-free hERG Channel
8ZYO 3.29 Å, Cryo-EM Structure of astemizole-bound hERG Channel
9CHP 3.3 Å, Cryo-EM structure of the human ether-a-go-go related K+ channel (hERG) in 300 mM K+
8IO4 3.5 Å, Herg1a-herg1b open state
9CHR 3.5 Å, Cryo-EM structure of the human ether-a-go-go related K+ channel (hERG) in 300 mM K+…
5VA1 3.7 Å, Cryo-EM structure of the human ether-a-go-go related K+ channel

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