8IO5: Herg1a-herg1b closed state 2

Herg1a-herg1b closed state 2. Determined by electron microscopy at 3.8 Å resolution. Released 13 Mar 2024.

Method: Electron microscopy
Resolution: 3.8 Å
Organism: Homo sapiens
Chains: 4
Atoms: 13,736
Mol. weight: 507.21 kDa
Released: 13 Mar 2024

Explore 8IO5 in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

8IO5 contains 72 α-helices and 36 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.

Chains A and D: 18 helices, 9 β-strands

Element	Residues	Length	Sheet
α-helix	399-401	3
α-helix	405-430	26
α-helix	452-472	21
α-helix	486-493	8
α-helix	497-504	8
α-helix	527-537	11
α-helix	539-542	4
α-helix	546-575	30
α-helix	585-592	8
α-helix	609-622	14
α-helix	635-686	52
α-helix	691-708	18
α-helix	713-719	7
α-helix	722-731	10
α-helix	741-744	4
α-helix	748-757	10
β-strand	759-761	3	1
β-strand	778-782	5	1
β-strand	788	1	2
β-strand	789-790	2	3
β-strand	795-796	2	3
β-strand	805-806	2	4
β-strand	823	1	2
β-strand	830-834	5	1
α-helix	837-842	6
α-helix	846-854	9
β-strand	860-861	2	4

Chains B and C: 18 helices, 9 β-strands

Element	Residues	Length	Sheet
α-helix	399-401	3
α-helix	405-430	26
α-helix	452-472	21
α-helix	486-493	8
α-helix	497-504	8
α-helix	527-537	11
α-helix	539-542	4
α-helix	546-575	30
α-helix	585-592	8
α-helix	609-622	14
α-helix	635-686	52
α-helix	691-707	17
α-helix	713-719	7
α-helix	722-731	10
α-helix	741-744	4
α-helix	748-757	10
β-strand	759-761	3	5
β-strand	778-782	5	5
β-strand	788	1	6
β-strand	789-790	2	7
β-strand	795-796	2	7
β-strand	805-806	2	8
β-strand	823	1	6
β-strand	830-834	5	5
α-helix	837-842	6
α-helix	846-854	9
β-strand	860-861	2	8

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Potassium voltage-gated channel subfamily H member 2	A, B, C, D	protein	1159	Homo sapiens	Q12809 (AlphaFold model)

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

>8IO5_1 Potassium voltage-gated channel subfamily H member 2 (chains A, B, C, D)
MPVRRGHVAPQNTFLDTIIRKFEGQSRKFIIANARVENCAVIYCNDGFCELCGYSRAEVM
QRPCTCDFLHGPRTQRRAAAQIAQALLGAEERKVEIAFYRKDGSCFLCLVDVVPVKNEDG
AVIMFILNFEVVMEKDMVGSPAHDTNHRGPPTSWLAPGRAKTFRLKLPALLALTARESSV
RSGGAGGAGAPGAVVVDVDLTPAAPSSESLALDEVTAMDNHVAGLGPAEERRALVGPGSP
PRSAPGQLPSPRAHSLNPDASGSSCSLARTRSRESCASVRRASSADDIEAMRAGVLPPPP
RHASTGAMHPLRSGLLNSTSDSDLVRYRTISKIPQITLNFVDLKGDPFLASPTSDREIIA
PKIKERTHNVTEKVTQVLSLGADVLPEYKLQAPRIHRWTILHYSPFKAVWDWLILLLVIY
TAVFTPYSAAFLLKETEEGPPATECGYACQPLAVVDLIVDIMFIVDILINFRTTYVNANE
EVVSHPGRIAVHYFKGWFLIDMVAAIPFDLLIFGSGSEELIGLLKTARLLRLVRVARKLD
RYSEYGAAVLFLLMCTFALIAHWLACIWYAIGNMEQPHMDSRIGWLHNLGDQIGKPYNSS
GLGGPSIKDKYVTALYFTFSSLTSVGFGNVSPNTNSEKIFSICVMLIGSLMYASIFGNVS
AIIQRLYSGTARYHTQMLRVREFIRFHQIPNPLRQRLEEYFQHAWSYTNGIDMNAVLKGF
PECLQADICLHLNRSLLQHCKPFRGATKGCLRALAMKFKTTHAPPGDTLVHAGDLLTALY
FISRGSIEILRGDVVVAILGKNDIFGEPLNLYARPGKSNGDVRALTYCDLHKIHRDDLLE
VLDMYPEFSDHFWSSLEITFNLRDTNMIPGSPGSTELEGGFSRQRKRKLSFRRRTDKDTE
QPGEVSALGPGRAGAGPSSRGRPGGPWGESPSSGPSSPESSEDEGPGRSSSPLRLVPFSS
PRPPGEPPGGEPLMEDCEKSSDTCNPLSGAFSGVSNIFSFWGDSRGRQYQELPRCPAPTP
SLLNIPLSSPGRRPRGDVESRLDALQRQLNRLETRLSADMATVLQLLQRQMTLVPPAYSA
VTTPGPGPTSTSPLLPVSPLPTLTLDSLSQVSQFMACEELPPGAPELPQEGPTRRLSLPG
QLGALTSQPLHRHGSDPGS

Primary citation

Structure of Herg1a-herg1b open state. Zhang, M.F. To be published.

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+
9CHS 3.4 Å, Cryo-EM structure of the human ether-a-go-go related K+ channel (hERG) in 3 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+…

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