8IOB: Herg1a-herg1b closed state 1

Herg1a-herg1b closed state 1. Determined by electron microscopy at 3.9 Å resolution. Released 13 Mar 2024.

Method: Electron microscopy
Resolution: 3.9 Å
Organism: Homo sapiens
Chains: 4
Atoms: 13,736
Mol. weight: 507.21 kDa
Released: 13 Mar 2024

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

Secondary structure: helices and β-sheets

8IOB contains 76 α-helices and 39 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: 19 helices, 9 β-strands

Element	Residues	Length	Sheet
α-helix	399	1
β-strand	400	1	1
α-helix	401	1
α-helix	405-430	26
α-helix	452-472	21
β-strand	473	1	1
α-helix	486-493	8
α-helix	497-505	9
α-helix	526-536	11
α-helix	539-542	4
α-helix	546-575	30
α-helix	585-592	8
α-helix	609-620	12
α-helix	635-686	52
α-helix	691-707	17
α-helix	713-719	7
α-helix	723-730	8
α-helix	742-745	4
α-helix	748-756	9
β-strand	759	1	2
β-strand	762-763	2	2
β-strand	780-785	6	2
β-strand	788-790	3	3
β-strand	795-796	2	3
β-strand	822-823	2	3
β-strand	828-832	5	2
α-helix	835-842	8
α-helix	846-854	9

Chain B: 19 helices, 8 β-strands

Element	Residues	Length	Sheet
α-helix	399	1
β-strand	400	1	4
α-helix	401	1
α-helix	405-430	26
α-helix	452-472	21
β-strand	473	1	4
α-helix	486-493	8
α-helix	497-505	9
α-helix	526-537	12
α-helix	539-542	4
α-helix	546-575	30
α-helix	585-592	8
α-helix	609-620	12
α-helix	635-686	52
α-helix	691-707	17
α-helix	713-719	7
α-helix	723-730	8
α-helix	742-745	4
α-helix	748-756	9
β-strand	759-763	5	5
β-strand	780-785	6	5
β-strand	788-790	3	6
β-strand	795-796	2	6
β-strand	822-823	2	6
β-strand	828-832	5	5
α-helix	835-843	9
α-helix	846-854	9

Chains C and D: 19 helices, 11 β-strands

Element	Residues	Length	Sheet
α-helix	399	1
β-strand	400	1	7
α-helix	401	1
α-helix	405-430	26
α-helix	452-472	21
β-strand	473	1	7
α-helix	486-493	8
α-helix	497-505	9
α-helix	526-537	12
α-helix	539-542	4
α-helix	546-575	30
α-helix	585-592	8
α-helix	609-620	12
α-helix	635-686	52
α-helix	691-707	17
α-helix	713-719	7
α-helix	723-730	8
α-helix	742-745	4
α-helix	748-756	9
β-strand	759	1	8
β-strand	762-763	2	8
β-strand	780-785	6	8
β-strand	788-790	3	9
β-strand	795-796	2	9
β-strand	805-806	2	10
β-strand	822-823	2	9
β-strand	828-832	5	8
α-helix	835-843	9
α-helix	846-854	9
β-strand	860-861	2	10

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

>8IOB_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 closed state 1. 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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